Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process thr...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Wan, Chanjuan [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2015 Elsevier Ireland Ltd. All rights reserved. |
|---|
| Schlagwörter: |
Vesicular Transport Proteins - chemistry |
|---|
| Übergeordnetes Werk: |
Enthalten in: Chemistry and physics of lipids - Shannon [u.a.] : Elsevier Scientific Publishers, 1966, 186(2015), Seite 61-67 |
|---|---|
| Übergeordnetes Werk: |
volume:186 ; year:2015 ; pages:61-67 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.chemphyslip.2015.01.003 |
|---|
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OLC1966944608 |
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| 520 | |a Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis. | ||
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10.1016/j.chemphyslip.2015.01.003 doi PQ20160617 (DE-627)OLC1966944608 (DE-599)GBVOLC1966944608 (PRQ)c1338-466109180ac847040b4dac6e93149b252481200fccbc7ae6b68a87fc1e714c3b0 (KEY)0065792120150000186000000061insightsintothemolecularrecognitionofthegranuphili DE-627 ger DE-627 rakwb eng 570 540 530 DNB Wan, Chanjuan verfasserin aut Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis. Nutzungsrecht: Copyright © 2015 Elsevier Ireland Ltd. All rights reserved. Vesicular Transport Proteins - chemistry Phosphatidylinositol Phosphates - metabolism Vesicular Transport Proteins - metabolism Wu, Bo oth Song, Zhenwei oth Zhang, Jiahai oth Chu, Huiying oth Wang, Aoli oth Liu, Qingsong oth Shi, Yunyu oth Li, Guohui oth Wang, Junfeng oth Enthalten in Chemistry and physics of lipids Shannon [u.a.] : Elsevier Scientific Publishers, 1966 186(2015), Seite 61-67 (DE-627)129526878 (DE-600)213869-4 (DE-576)014946831 0009-3084 nnns volume:186 year:2015 pages:61-67 http://dx.doi.org/10.1016/j.chemphyslip.2015.01.003 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25595293 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 AR 186 2015 61-67 |
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10.1016/j.chemphyslip.2015.01.003 doi PQ20160617 (DE-627)OLC1966944608 (DE-599)GBVOLC1966944608 (PRQ)c1338-466109180ac847040b4dac6e93149b252481200fccbc7ae6b68a87fc1e714c3b0 (KEY)0065792120150000186000000061insightsintothemolecularrecognitionofthegranuphili DE-627 ger DE-627 rakwb eng 570 540 530 DNB Wan, Chanjuan verfasserin aut Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis. Nutzungsrecht: Copyright © 2015 Elsevier Ireland Ltd. All rights reserved. Vesicular Transport Proteins - chemistry Phosphatidylinositol Phosphates - metabolism Vesicular Transport Proteins - metabolism Wu, Bo oth Song, Zhenwei oth Zhang, Jiahai oth Chu, Huiying oth Wang, Aoli oth Liu, Qingsong oth Shi, Yunyu oth Li, Guohui oth Wang, Junfeng oth Enthalten in Chemistry and physics of lipids Shannon [u.a.] : Elsevier Scientific Publishers, 1966 186(2015), Seite 61-67 (DE-627)129526878 (DE-600)213869-4 (DE-576)014946831 0009-3084 nnns volume:186 year:2015 pages:61-67 http://dx.doi.org/10.1016/j.chemphyslip.2015.01.003 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25595293 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_4012 AR 186 2015 61-67 |
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Chemistry and physics of lipids |
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Chemistry and physics of lipids |
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Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2 |
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Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2 |
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Wan, Chanjuan |
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Chemistry and physics of lipids |
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Chemistry and physics of lipids |
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Wan, Chanjuan |
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10.1016/j.chemphyslip.2015.01.003 |
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insights into the molecular recognition of the granuphilin c2a domain with pi(4,5)p2 |
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Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2 |
| abstract |
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis. |
| abstractGer |
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis. |
| abstract_unstemmed |
Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a key player in regulating the process of excytosis, including insulin secretion. Granuphilin, a tandem C2 domain containing protein, mediates the docking of insulin granules onto plasma membrane. The C2A domain plays key roles in this process through interaction with PI(4,5)P2. In this study, we have investigated the molecular recognition mechanism of granuphilin-C2A domain to PI(4,5)P2 head group, and further to PI(4,5)P2-nanodisc by NMR, ITC, MST and SEC methods. Our results demonstrate that PI(4,5)P2 binds to the concave surface of granuphilin-C2A domain. The key residues involved in the binding were validated by mutation analysis. |
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| title_short |
Insights into the molecular recognition of the granuphilin C2A domain with PI(4,5)P2 |
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http://dx.doi.org/10.1016/j.chemphyslip.2015.01.003 http://www.ncbi.nlm.nih.gov/pubmed/25595293 |
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Wu, Bo Song, Zhenwei Zhang, Jiahai Chu, Huiying Wang, Aoli Liu, Qingsong Shi, Yunyu Li, Guohui Wang, Junfeng |
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