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    SEC14 phosphatidylinositol/phosphatidylcholine transfer protein SEC14 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855103, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Biophysical parameters of the Sec14 phospholipid exchange cycle - Effect of lipid packing in membranes.

    Biophysical parameters of the Sec14 phospholipid exchange cycle - Effect of lipid packing in membranes.
    Sugiura T, Nakao H, Ikeda K, Khan D, Nile AH, Bankaitis VA, Nakano M., Free PMC Article

    04/17/2021
    Noncanonical regulation of phosphatidylserine metabolism by a Sec14-like protein and a lipid kinase.

    Noncanonical regulation of phosphatidylserine metabolism by a Sec14-like protein and a lipid kinase.
    Wang Y, Yuan P, Grabon A, Tripathi A, Lee D, Rodriguez M, Lönnfors M, Eisenberg-Bord M, Wang Z, Man Lam S, Schuldiner M, Bankaitis VA., Free PMC Article

    02/20/2021
    yeast Sec14-like PITP lipid-binding pockets indeed define diverse chemical microenvironments that translate into differential ligand-binding specificities across this protein family

    Functional diversification of the chemical landscapes of yeast Sec14-like phosphatidylinositol transfer protein lipid-binding cavities.
    Tripathi A, Martinez E, Obaidullah AJ, Lete MG, Lönnfors M, Khan D, Soni KG, Mousley CJ, Kellogg GE, Bankaitis VA., Free PMC Article

    07/18/2020
    Data suggest that SEC14L and SFH1 undergo conformational changes as phosphatidylinositol/phosphatidylcholine bind to hydrophobic pockets/ligand binding sites. [review-like article]

    Sec14-like phosphatidylinositol-transfer proteins and diversification of phosphoinositide signalling outcomes.
    Tripathi A, Nile AH, Bankaitis VA., Free PMC Article

    06/6/2015
    Sec14 and Sec14 like proteins form central conduits to integrate multiple aspects of lipid metabolism with productive phosphoinositide signaling. (Review)

    Sec14 like PITPs couple lipid metabolism with phosphoinositide synthesis to regulate Golgi functionality.
    Mousley CJ, Davison JM, Bankaitis VA., Free PMC Article

    01/24/2015
    The crystal structure of Sec14 family homologue (Sfh)3 is the first report of a dimeric Sec14 protein and provides clues for its functional study.

    Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding.
    Yuan Y, Zhao W, Wang X, Gao Y, Niu L, Teng M.

    08/3/2013
    Localization of lipid raft proteins to the plasma membrane is a major function of the phospholipid transfer protein Sec14.

    Localization of lipid raft proteins to the plasma membrane is a major function of the phospholipid transfer protein Sec14.
    Curwin AJ, Leblanc MA, Fairn GD, McMaster CR., Free PMC Article

    07/27/2013
    To launch a detailed structural and functional characterization of Sfh3, the recombinant protein was purified to homogeneity, diffraction-quality crystals were produced and a native X-ray data set was collected to 2.2 A resolution

    Crystallization and preliminary X-ray diffraction analysis of Sfh3, a member of the Sec14 protein superfamily.
    Ren J, Schaaf G, Bankaitis VA, Ortlund EA, Pathak MC., Free PMC Article

    02/4/2012
    Sec14 function was required for the route followed by Bgl2, whereas trafficking of other secreted proteins, including Hsp150, Cts1, Scw4, Scw10, Exg1, Cis3, and Ygp1, still occurred, indicating Sec14 regulates specific trans-Golgi export pathways.

    Phospholipid transfer protein Sec14 is required for trafficking from endosomes and regulates distinct trans-Golgi export pathways.
    Curwin AJ, Fairn GD, McMaster CR., Free PMC Article

    01/21/2010
    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

    Functional anatomy of phospholipid binding and regulation of phosphoinositide homeostasis by proteins of the sec14 superfamily.
    Schaaf G, Ortlund EA, Tyeryar KR, Mousley CJ, Ile KE, Garrett TA, Ren J, Woolls MJ, Raetz CR, Redinbo MR, Bankaitis VA., Free PMC Article

    01/21/2010
    Sec14p regulation of phosphoinositide levels affects cytokinesis at the level of the Cdc42p/Cla4p/Ste20p signaling cascade.

    Regulation of phosphoinositide levels by the phospholipid transfer protein Sec14p controls Cdc42p/p21-activated kinase-mediated cell cycle progression at cytokinesis.
    Howe AG, Fairn GD, MacDonald K, Bankaitis VA, McMaster CR., Free PMC Article

    01/21/2010
    This review describes Sec14p, the major (phosphatidylinositol)/PC (phosphatidylcholine)-transfer protein in yeast, which co-ordinates lipid metabolism with protein transport from the Golgi complex.

    Sec14p-like proteins regulate phosphoinositide homoeostasis and intracellular protein and lipid trafficking in yeast.
    Mousley CJ, Tyeryar KR, Ryan MM, Bankaitis VA.

    01/21/2010
    Sec14 protein is a peripheral Golgi membrane protein essential for Golgi secretory function and cell viability[review].

    Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae.
    Bankaitis VA, Phillips S, Yanagisawa L, Li X, Routt S, Xie Z.

    01/21/2010
    The application of EPR spectrscopy to investigate the chemical properties of binding between phosphatidylcholine and Sec14 is reported.

    The chemistry of phospholipid binding by the Saccharomyces cerevisiae phosphatidylinositol transfer protein Sec14p as determined by EPR spectroscopy.
    Smirnova TI, Chadwick TG, MacArthur R, Poluektov O, Song L, Ryan MM, Schaaf G, Bankaitis VA.

    01/21/2010
    molecular dynamics suggests large rigid body motions within Sec14p accompany closing and opening of an A(10)/T(4)/A(11) helical gate, and that "state-of-closure" of this helical gate determines access to the Sec14p phospholipid binding cavity

    Conformational dynamics of the major yeast phosphatidylinositol transfer protein sec14p: insight into the mechanisms of phospholipid exchange and diseases of sec14p-like protein deficiencies.
    Ryan MM, Temple BR, Phillips SE, Bankaitis VA., Free PMC Article

    01/21/2010
    Sec14p acts as a positive regulator of Nte1p-mediated PC deacylation with the functional consequence of increased Nte1p activity increasing the permissive temperature for the growth of sec14(ts) cells

    Nte1p-mediated deacylation of phosphatidylcholine functionally interacts with Sec14p.
    Murray JP, McMaster CR.

    01/21/2010
    This review focuses on five yeast proteins that share significant sequence homology with Sec14p and have distinct subcellular localizations with functions related to lipid metabolism, phosphoinositide mediated signaling and membrane trafficking.

    Sec14 related proteins in yeast.
    Griac P.

    01/21/2010
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