Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3
The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Hashimoto, Yoshifumi [verfasserIn] |
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| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. |
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| Schlagwörter: |
inhibitor of apoptosis protein Peptide Termination Factors - genetics |
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| Übergeordnetes Werk: |
Enthalten in: FEBS letters - Amsterdam [u.a.] : Elsevier, 1968, 589(2015), 17, Seite 2241-2247 |
|---|---|
| Übergeordnetes Werk: |
volume:589 ; year:2015 ; number:17 ; pages:2241-2247 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.febslet.2015.06.041 |
|---|
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| 520 | |a The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. | ||
| 540 | |a Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies | ||
| 540 | |a Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | ||
| 650 | 4 | |a Calpain | |
| 650 | 4 | |a Apoptosis | |
| 650 | 4 | |a eRF3 | |
| 650 | 4 | |a IAP | |
| 650 | 4 | |a inhibitor of apoptosis protein | |
| 650 | 4 | |a Translation termination | |
| 650 | 4 | |a Peptide Termination Factors - genetics | |
| 650 | 4 | |a Protein Isoforms - metabolism | |
| 650 | 4 | |a Calcium - metabolism | |
| 650 | 4 | |a Peptide Termination Factors - metabolism | |
| 650 | 4 | |a Calpain - metabolism | |
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| 700 | 1 | |a Inagaki, Hiroto |4 oth | |
| 700 | 1 | |a Hoshino, Shin-ichi |4 oth | |
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10.1016/j.febslet.2015.06.041 doi PQ20160617 (DE-627)OLC1965548458 (DE-599)GBVOLC1965548458 (PRQ)p1775-5c070aaa2a0fe5718ee24dde67cce1c45b64e83678a54aabc398bde6813354ed0 (KEY)0045922420150000589001702241calpainmediatesprocessingofthetranslationterminati DE-627 ger DE-627 rakwb eng 570 530 610 DNB Hashimoto, Yoshifumi verfasserin aut Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Calpain Apoptosis eRF3 IAP inhibitor of apoptosis protein Translation termination Peptide Termination Factors - genetics Protein Isoforms - metabolism Calcium - metabolism Peptide Termination Factors - metabolism Calpain - metabolism X-Linked Inhibitor of Apoptosis Protein - metabolism Inagaki, Hiroto oth Hoshino, Shin-ichi oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 17, Seite 2241-2247 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:17 pages:2241-2247 http://dx.doi.org/10.1016/j.febslet.2015.06.041 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.041/abstract http://www.ncbi.nlm.nih.gov/pubmed/26172506 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 17 2241-2247 |
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10.1016/j.febslet.2015.06.041 doi PQ20160617 (DE-627)OLC1965548458 (DE-599)GBVOLC1965548458 (PRQ)p1775-5c070aaa2a0fe5718ee24dde67cce1c45b64e83678a54aabc398bde6813354ed0 (KEY)0045922420150000589001702241calpainmediatesprocessingofthetranslationterminati DE-627 ger DE-627 rakwb eng 570 530 610 DNB Hashimoto, Yoshifumi verfasserin aut Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Calpain Apoptosis eRF3 IAP inhibitor of apoptosis protein Translation termination Peptide Termination Factors - genetics Protein Isoforms - metabolism Calcium - metabolism Peptide Termination Factors - metabolism Calpain - metabolism X-Linked Inhibitor of Apoptosis Protein - metabolism Inagaki, Hiroto oth Hoshino, Shin-ichi oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 17, Seite 2241-2247 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:17 pages:2241-2247 http://dx.doi.org/10.1016/j.febslet.2015.06.041 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.041/abstract http://www.ncbi.nlm.nih.gov/pubmed/26172506 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 17 2241-2247 |
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10.1016/j.febslet.2015.06.041 doi PQ20160617 (DE-627)OLC1965548458 (DE-599)GBVOLC1965548458 (PRQ)p1775-5c070aaa2a0fe5718ee24dde67cce1c45b64e83678a54aabc398bde6813354ed0 (KEY)0045922420150000589001702241calpainmediatesprocessingofthetranslationterminati DE-627 ger DE-627 rakwb eng 570 530 610 DNB Hashimoto, Yoshifumi verfasserin aut Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Calpain Apoptosis eRF3 IAP inhibitor of apoptosis protein Translation termination Peptide Termination Factors - genetics Protein Isoforms - metabolism Calcium - metabolism Peptide Termination Factors - metabolism Calpain - metabolism X-Linked Inhibitor of Apoptosis Protein - metabolism Inagaki, Hiroto oth Hoshino, Shin-ichi oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 17, Seite 2241-2247 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:17 pages:2241-2247 http://dx.doi.org/10.1016/j.febslet.2015.06.041 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.041/abstract http://www.ncbi.nlm.nih.gov/pubmed/26172506 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 17 2241-2247 |
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10.1016/j.febslet.2015.06.041 doi PQ20160617 (DE-627)OLC1965548458 (DE-599)GBVOLC1965548458 (PRQ)p1775-5c070aaa2a0fe5718ee24dde67cce1c45b64e83678a54aabc398bde6813354ed0 (KEY)0045922420150000589001702241calpainmediatesprocessingofthetranslationterminati DE-627 ger DE-627 rakwb eng 570 530 610 DNB Hashimoto, Yoshifumi verfasserin aut Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Calpain Apoptosis eRF3 IAP inhibitor of apoptosis protein Translation termination Peptide Termination Factors - genetics Protein Isoforms - metabolism Calcium - metabolism Peptide Termination Factors - metabolism Calpain - metabolism X-Linked Inhibitor of Apoptosis Protein - metabolism Inagaki, Hiroto oth Hoshino, Shin-ichi oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 17, Seite 2241-2247 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:17 pages:2241-2247 http://dx.doi.org/10.1016/j.febslet.2015.06.041 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.041/abstract http://www.ncbi.nlm.nih.gov/pubmed/26172506 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 17 2241-2247 |
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10.1016/j.febslet.2015.06.041 doi PQ20160617 (DE-627)OLC1965548458 (DE-599)GBVOLC1965548458 (PRQ)p1775-5c070aaa2a0fe5718ee24dde67cce1c45b64e83678a54aabc398bde6813354ed0 (KEY)0045922420150000589001702241calpainmediatesprocessingofthetranslationterminati DE-627 ger DE-627 rakwb eng 570 530 610 DNB Hashimoto, Yoshifumi verfasserin aut Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. Nutzungsrecht: FEBS Letters 589 (2015) 1873-3468 © 2015 Federation of European Biochemical Societies Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Calpain Apoptosis eRF3 IAP inhibitor of apoptosis protein Translation termination Peptide Termination Factors - genetics Protein Isoforms - metabolism Calcium - metabolism Peptide Termination Factors - metabolism Calpain - metabolism X-Linked Inhibitor of Apoptosis Protein - metabolism Inagaki, Hiroto oth Hoshino, Shin-ichi oth Enthalten in FEBS letters Amsterdam [u.a.] : Elsevier, 1968 589(2015), 17, Seite 2241-2247 (DE-627)129522023 (DE-600)212746-5 (DE-576)014938014 0014-5793 nnns volume:589 year:2015 number:17 pages:2241-2247 http://dx.doi.org/10.1016/j.febslet.2015.06.041 Volltext http://onlinelibrary.wiley.com/doi/10.1016/j.febslet.2015.06.041/abstract http://www.ncbi.nlm.nih.gov/pubmed/26172506 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_21 GBV_ILN_70 GBV_ILN_211 GBV_ILN_2219 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 AR 589 2015 17 2241-2247 |
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Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 |
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Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 |
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The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. |
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The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. |
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The involvement of polypeptide chain‐releasing factor eRF3 in translation termination and mRNA decay is well established. Moreover, the finding that the proteolytically processed isoform of eRF3 (p‐eRF3) interacts with inhibitors of apoptosis proteins (IAPs) to activate caspase, implies that eRF3 is a cell death regulator. However, the protease(s) responsible for p‐eRF3 production and how p‐eRF3 regulates apoptosis remain unknown. Here, we show that calpain mediates p‐eRF3 production in vitro and in living cells. p‐eRF3 is produced in cells treated with ER stressors in a calpain‐dependent manner. These findings suggest that p‐eRF3 is a novel regulator of calpain‐dependent cell death. Calpain is responsible for processing eRF3 into its IAP‐binding isoform p‐eRF3. Calpain mediates ER‐stress‐induced production of p‐eRF3. p‐eRF3 is a novel regulator of calpain‐dependent cell death. |
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Calpain mediates processing of the translation termination factor eRF3 into the IAP‐binding isoform p‐eRF3 |
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