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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/A0A140UHP8_9PEZI A0A140UHP8_9PEZI] | | [https://www.uniprot.org/uniprot/A0A140UHP8_9PEZI A0A140UHP8_9PEZI] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The Golgi complex is the central sorting compartment of eukaryotic cells. Arf guanine nucleotide exchange factors (Arf-GEFs) regulate virtually all traffic through the Golgi by activating Arf GTPase trafficking pathways. The Golgi Arf-GEFs contain multiple autoregulatory domains, but the precise mechanisms underlying their function remain largely undefined. We report a crystal structure revealing that the N-terminal DCB and HUS regulatory domains of the Arf-GEF Sec7 form a single structural unit. We demonstrate that the established role of the N-terminal region in dimerization is not conserved; instead, a C-terminal autoinhibitory domain is responsible for dimerization of Sec7. We find that the DCB/HUS domain amplifies the ability of Sec7 to activate Arf1 on the membrane surface by facilitating membrane insertion of the Arf1 amphipathic helix. This enhancing function of the Sec7 N-terminal domains is consistent with the high rate of Arf1-dependent trafficking to the plasma membrane necessary for maximal cell growth.
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| The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.,Richardson BC, Halaby SL, Gustafson MA, Fromme JC Elife. 2016 Jan 14;5. pii: e12411. doi: 10.7554/eLife.12411. PMID:26765562<ref>PMID:26765562</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5has" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
