Defects in autophagy caused by glaucoma-associated mutations in optineurin
Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link t...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Sirohi, Kapil [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Schlagwörter: |
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| Umfang: |
10 |
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| Übergeordnetes Werk: |
Enthalten in: Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary - Billo, Georis ELSEVIER, 2022, official journal of the ISER, Amsterdam [u.a.] |
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| Übergeordnetes Werk: |
volume:144 ; year:2016 ; pages:54-63 ; extent:10 |
| Links: |
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| DOI / URN: |
10.1016/j.exer.2015.08.020 |
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ELV019817851 |
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| 245 | 1 | 0 | |a Defects in autophagy caused by glaucoma-associated mutations in optineurin |
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| 520 | |a Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. | ||
| 520 | |a Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. | ||
| 650 | 7 | |a Glaucoma |2 Elsevier | |
| 650 | 7 | |a Mutations |2 Elsevier | |
| 650 | 7 | |a Optineurin |2 Elsevier | |
| 650 | 7 | |a M98K-OPTN |2 Elsevier | |
| 650 | 7 | |a E50K-OPTN |2 Elsevier | |
| 650 | 7 | |a Autophagy |2 Elsevier | |
| 700 | 1 | |a Swarup, Ghanshyam |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Billo, Georis ELSEVIER |t Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary |d 2022 |d official journal of the ISER |g Amsterdam [u.a.] |w (DE-627)ELV008415374 |
| 773 | 1 | 8 | |g volume:144 |g year:2016 |g pages:54-63 |g extent:10 |
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2016transfer abstract |
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2016 |
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10.1016/j.exer.2015.08.020 doi GBVA2016021000017.pica (DE-627)ELV019817851 (ELSEVIER)S0014-4835(15)30016-6 DE-627 ger DE-627 rakwb eng 610 610 DE-600 510 004 VZ 31.80 bkl 54.80 bkl Sirohi, Kapil verfasserin aut Defects in autophagy caused by glaucoma-associated mutations in optineurin 2016transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Glaucoma Elsevier Mutations Elsevier Optineurin Elsevier M98K-OPTN Elsevier E50K-OPTN Elsevier Autophagy Elsevier Swarup, Ghanshyam oth Enthalten in Elsevier Billo, Georis ELSEVIER Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary 2022 official journal of the ISER Amsterdam [u.a.] (DE-627)ELV008415374 volume:144 year:2016 pages:54-63 extent:10 https://doi.org/10.1016/j.exer.2015.08.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.80 Angewandte Mathematik VZ 54.80 Angewandte Informatik VZ AR 144 2016 54-63 10 045F 610 |
| spelling |
10.1016/j.exer.2015.08.020 doi GBVA2016021000017.pica (DE-627)ELV019817851 (ELSEVIER)S0014-4835(15)30016-6 DE-627 ger DE-627 rakwb eng 610 610 DE-600 510 004 VZ 31.80 bkl 54.80 bkl Sirohi, Kapil verfasserin aut Defects in autophagy caused by glaucoma-associated mutations in optineurin 2016transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Glaucoma Elsevier Mutations Elsevier Optineurin Elsevier M98K-OPTN Elsevier E50K-OPTN Elsevier Autophagy Elsevier Swarup, Ghanshyam oth Enthalten in Elsevier Billo, Georis ELSEVIER Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary 2022 official journal of the ISER Amsterdam [u.a.] (DE-627)ELV008415374 volume:144 year:2016 pages:54-63 extent:10 https://doi.org/10.1016/j.exer.2015.08.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.80 Angewandte Mathematik VZ 54.80 Angewandte Informatik VZ AR 144 2016 54-63 10 045F 610 |
| allfields_unstemmed |
10.1016/j.exer.2015.08.020 doi GBVA2016021000017.pica (DE-627)ELV019817851 (ELSEVIER)S0014-4835(15)30016-6 DE-627 ger DE-627 rakwb eng 610 610 DE-600 510 004 VZ 31.80 bkl 54.80 bkl Sirohi, Kapil verfasserin aut Defects in autophagy caused by glaucoma-associated mutations in optineurin 2016transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Glaucoma Elsevier Mutations Elsevier Optineurin Elsevier M98K-OPTN Elsevier E50K-OPTN Elsevier Autophagy Elsevier Swarup, Ghanshyam oth Enthalten in Elsevier Billo, Georis ELSEVIER Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary 2022 official journal of the ISER Amsterdam [u.a.] (DE-627)ELV008415374 volume:144 year:2016 pages:54-63 extent:10 https://doi.org/10.1016/j.exer.2015.08.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.80 Angewandte Mathematik VZ 54.80 Angewandte Informatik VZ AR 144 2016 54-63 10 045F 610 |
| allfieldsGer |
10.1016/j.exer.2015.08.020 doi GBVA2016021000017.pica (DE-627)ELV019817851 (ELSEVIER)S0014-4835(15)30016-6 DE-627 ger DE-627 rakwb eng 610 610 DE-600 510 004 VZ 31.80 bkl 54.80 bkl Sirohi, Kapil verfasserin aut Defects in autophagy caused by glaucoma-associated mutations in optineurin 2016transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Glaucoma Elsevier Mutations Elsevier Optineurin Elsevier M98K-OPTN Elsevier E50K-OPTN Elsevier Autophagy Elsevier Swarup, Ghanshyam oth Enthalten in Elsevier Billo, Georis ELSEVIER Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary 2022 official journal of the ISER Amsterdam [u.a.] (DE-627)ELV008415374 volume:144 year:2016 pages:54-63 extent:10 https://doi.org/10.1016/j.exer.2015.08.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.80 Angewandte Mathematik VZ 54.80 Angewandte Informatik VZ AR 144 2016 54-63 10 045F 610 |
| allfieldsSound |
10.1016/j.exer.2015.08.020 doi GBVA2016021000017.pica (DE-627)ELV019817851 (ELSEVIER)S0014-4835(15)30016-6 DE-627 ger DE-627 rakwb eng 610 610 DE-600 510 004 VZ 31.80 bkl 54.80 bkl Sirohi, Kapil verfasserin aut Defects in autophagy caused by glaucoma-associated mutations in optineurin 2016transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. Glaucoma Elsevier Mutations Elsevier Optineurin Elsevier M98K-OPTN Elsevier E50K-OPTN Elsevier Autophagy Elsevier Swarup, Ghanshyam oth Enthalten in Elsevier Billo, Georis ELSEVIER Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary 2022 official journal of the ISER Amsterdam [u.a.] (DE-627)ELV008415374 volume:144 year:2016 pages:54-63 extent:10 https://doi.org/10.1016/j.exer.2015.08.020 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT 31.80 Angewandte Mathematik VZ 54.80 Angewandte Informatik VZ AR 144 2016 54-63 10 045F 610 |
| language |
English |
| source |
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defects in autophagy caused by glaucoma-associated mutations in optineurin |
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Defects in autophagy caused by glaucoma-associated mutations in optineurin |
| abstract |
Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. |
| abstractGer |
Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. |
| abstract_unstemmed |
Certain mutations in optineurin (gene OPTN) are associated with primary open angle glaucoma. Optineurin is ubiquitously expressed but it shows high level of expression in certain cells and tissues including retinal ganglion cells. It interacts with many proteins, often acting as an adaptor to link two or more proteins. These interactions play a crucial role in mediating various functions of optineurin such as membrane vesicle trafficking, autophagy, signal transduction etc. Autophagy is basically a quality control mechanism to remove damaged proteins and organelles through lysosomal degradation. Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored. |
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Optineurin was identified as an autophagy receptor that directly interacts with autophagosomal protein, LC3, and ubiquitin. These interactions are important for autophagy receptor function. Autophagy receptors recruit their cargo and take it to autophagosomes which fuse with lysosomes to form autolysosomes where degradation of proteins takes place. Optineurin interacts with a motor protein, myosinVI, and this interaction is involved in mediating fusion of autophagosomes with lysosomes. A glaucoma-associated mutant of optineurin, E50K, impairs autophagy as well as vesicle trafficking, leading to death of retinal cells by apoptosis. E50K-OPTN-induced block in autophagy is dependent on a GTPase activating protein, TBC1D17. The E50K mutant also causes other changes in the cells such as altered interaction with TBK1 protein kinase, aggregate formation, generation of reactive oxygen species and inhibition of proteasome, which may contribute to pathogenesis. A polymorphism of optineurin, M98K, associated with glaucoma, causes enhanced autophagy leading to transferrin receptor degradation and apoptotic death of retinal cells. M98K-OPTN-induced autophagic cell death is dependent on Rab12 GTPase. Thus, an optimum level of optineurin-mediated autophagy is crucial for survival of retinal cells, and impaired autophagy is likely to contribute to glaucoma pathogenesis. How impaired autophagy caused by optineurin mutants leads to apoptosis and cell death, is yet to be explored.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Glaucoma</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Mutations</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Optineurin</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">M98K-OPTN</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">E50K-OPTN</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Autophagy</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Swarup, Ghanshyam</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier</subfield><subfield code="a">Billo, Georis ELSEVIER</subfield><subfield code="t">Comparison of several interpolation methods to reconstruct field data in the vicinity of a finite element immersed boundary</subfield><subfield code="d">2022</subfield><subfield code="d">official journal of the ISER</subfield><subfield code="g">Amsterdam [u.a.]</subfield><subfield code="w">(DE-627)ELV008415374</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:144</subfield><subfield code="g">year:2016</subfield><subfield code="g">pages:54-63</subfield><subfield code="g">extent:10</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.exer.2015.08.020</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OPC-MAT</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">31.80</subfield><subfield code="j">Angewandte Mathematik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">54.80</subfield><subfield code="j">Angewandte Informatik</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">144</subfield><subfield code="j">2016</subfield><subfield code="h">54-63</subfield><subfield code="g">10</subfield></datafield><datafield tag="953" ind1=" " ind2=" "><subfield code="2">045F</subfield><subfield code="a">610</subfield></datafield></record></collection>
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