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    Functional Anatomy of Phospholipid Binding and Regulation of Phosphoinositide Homeostasis by Proteins of the Sec14 Superfamily

    Access Status
    Open access via publisher
    Authors
    Schaaf, G.
    Ortlund, E.
    Tyeryar, K.
    Mousley, Carl
    Ile, K.
    Garrett, T.
    Ren, J.
    Woolls, M.
    Raetz, C.
    Redinbo, M.
    Bankaitis, V.
    Date
    2008
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Schaaf, G. and Ortlund, E. and Tyeryar, K. and Mousley, C. and Ile, K. and Garrett, T. and Ren, J. et al. 2008. Functional Anatomy of Phospholipid Binding and Regulation of Phosphoinositide Homeostasis by Proteins of the Sec14 Superfamily. Molecular Cell. 29 (2): pp. 191-206.
    Source Title
    Molecular Cell
    DOI
    10.1016/j.molcel.2007.11.026
    ISSN
    1097-2765
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/45619
    Collection
    • Curtin Research Publications
    Abstract

    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. © 2008 Elsevier Inc. All rights reserved.

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