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| {{STRUCTURE_3b74| PDB=3b74 | SCENE= }} | | {{STRUCTURE_3b74| PDB=3b74 | SCENE= }} |
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| '''Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylethanolamine'''
| | ===Crystal Structure of Yeast Sec14 Homolog Sfh1 in Complex with Phosphatidylethanolamine=== |
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| ==Overview==
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| Sec14, the major yeast phosphatidylinositol (PtdIns)/phosphatidylcholine (PtdCho) transfer protein, regulates essential interfaces between lipid metabolism and membrane trafficking from the trans-Golgi network (TGN). How Sec14 does so remains unclear. We report that Sec14 binds PtdIns and PtdCho at distinct (but overlapping) sites, and both PtdIns- and PtdCho-binding activities are essential Sec14 activities. We further show both activities must reside within the same molecule to reconstitute a functional Sec14 and for effective Sec14-mediated regulation of phosphoinositide homeostasis in vivo. This regulation is uncoupled from PtdIns-transfer activity and argues for an interfacial presentation mode for Sec14-mediated potentiation of PtdIns kinases. Such a regulatory role for Sec14 is a primary counter to action of the Kes1 sterol-binding protein that antagonizes PtdIns 4-OH kinase activity in vivo. Collectively, these findings outline functional mechanisms for the Sec14 superfamily and reveal additional layers of complexity for regulating phosphoinositide homeostasis in eukaryotes.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18243114}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18243114 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18243114}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sec14]] | | [[Category: Sec14]] |
| [[Category: Signaling protein]] | | [[Category: Signaling protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:27:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:43:15 2008'' |
