期刊
MOLECULAR CELL
卷 29, 期 2, 页码 191-206出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.11.026
关键词
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资金
- NIAID NIH HHS [5T32 AI 052080, T32 AI052080] Funding Source: Medline
- NIDDK NIH HHS [R01 DK062229, DK 62229] Funding Source: Medline
- NIGMS NIH HHS [GM 069338, U54 GM069338, R01 GM044530, GM 44530] Funding Source: Medline
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 Sec-14 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.
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