Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1
Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC)..
Adenosine diphosphate-ribosylation factor (Arf) guanosine triphosphatase-activating proteins (GAPs) are enzymes that need to bind to membranes to catalyze the hydrolysis of guanosine triphosphate (GTP) bound to the small GTP-binding protein Arf. Binding of the pleckstrin homology (PH) domain of the ArfGAP With SH3 domain, ankyrin repeat and PH domain 1 (ASAP1) to membranes containing phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] is key for maximum GTP hydrolysis but not fully understood. By combining nuclear magnetic resonance, neutron reflectometry, and molecular dynamics simulation, we show that binding of multiple PI(4,5)P2 molecules to the ASAP1 PH domain (i) triggers a functionally relevant allosteric conformational switch and (ii) maintains the PH domain in a well-defined orientation, allowing critical contacts with an Arf1 mimic to occur. Our model provides a framework to understand how binding of the ASAP1 PH domain to PI(4,5)P2 at the membrane may play a role in the regulation of ASAP1.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:6 |
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| Enthalten in: |
Science advances - 6(2020), 40 vom: 30. Sept. |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Soubias, Olivier [VerfasserIn] |
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| Links: |
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| Themen: |
Journal Article |
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| Anmerkungen: |
Date Revised 13.04.2022 published: Electronic-Print Citation Status PubMed-not-MEDLINE |
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| doi: |
10.1126/sciadv.abd1882 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM315693886 |
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| 100 | 1 | |a Soubias, Olivier |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Membrane surface recognition by the ASAP1 PH domain and consequences for interactions with the small GTPase Arf1 |
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| 500 | |a published: Electronic-Print | ||
| 500 | |a Citation Status PubMed-not-MEDLINE | ||
| 520 | |a Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). | ||
| 520 | |a Adenosine diphosphate-ribosylation factor (Arf) guanosine triphosphatase-activating proteins (GAPs) are enzymes that need to bind to membranes to catalyze the hydrolysis of guanosine triphosphate (GTP) bound to the small GTP-binding protein Arf. Binding of the pleckstrin homology (PH) domain of the ArfGAP With SH3 domain, ankyrin repeat and PH domain 1 (ASAP1) to membranes containing phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] is key for maximum GTP hydrolysis but not fully understood. By combining nuclear magnetic resonance, neutron reflectometry, and molecular dynamics simulation, we show that binding of multiple PI(4,5)P2 molecules to the ASAP1 PH domain (i) triggers a functionally relevant allosteric conformational switch and (ii) maintains the PH domain in a well-defined orientation, allowing critical contacts with an Arf1 mimic to occur. Our model provides a framework to understand how binding of the ASAP1 PH domain to PI(4,5)P2 at the membrane may play a role in the regulation of ASAP1 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
| 650 | 4 | |a Research Support, N.I.H., Intramural | |
| 700 | 1 | |a Pant, Shashank |e verfasserin |4 aut | |
| 700 | 1 | |a Heinrich, Frank |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Yue |e verfasserin |4 aut | |
| 700 | 1 | |a Roy, Neeladri Sekhar |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Jess |e verfasserin |4 aut | |
| 700 | 1 | |a Jian, Xiaoying |e verfasserin |4 aut | |
| 700 | 1 | |a Yohe, Marielle E |e verfasserin |4 aut | |
| 700 | 1 | |a Randazzo, Paul A |e verfasserin |4 aut | |
| 700 | 1 | |a Lösche, Mathias |e verfasserin |4 aut | |
| 700 | 1 | |a Tajkhorshid, Emad |e verfasserin |4 aut | |
| 700 | 1 | |a Byrd, R Andrew |e verfasserin |4 aut | |
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| 856 | 4 | 0 | |u http://dx.doi.org/10.1126/sciadv.abd1882 |3 Volltext |
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