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SEC14  -  phosphatidylinositol/phosphatidylcholine...

Saccharomyces cerevisiae S288c

Synonyms: PI/PC TP, PIT1, Phosphatidylinositol/phosphatidylcholine transfer protein, SEC14 cytosolic factor, YM9582.04, ...
 
 
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Disease relevance of SEC14

  • These findings indicate that Sec14p functions to alleviate a CDP-choline pathway-mediated toxicity to yeast Golgi secretory function [1].
 

High impact information on SEC14

  • The antagonistic action of the CKI gene product on SEC14p function revealed a previously unsuspected influence of biosynthetic activities of the CDP-choline pathway for PC biosynthesis on yeast Golgi function and indicated that SEC14p controls the phospholipid content of yeast Golgi membranes in vivo [2].
  • The yeast phosphatidylinositol-transfer protein (Sec14) catalyses exchange of phosphatidylinositol and phosphatidylcholine between membrane bilayers in vitro [3].
  • In vivo, Sec14 activity is essential for vesicle budding from the Golgi complex [3].
  • Here we show that defects in Sac1p also relieve the requirement for Sec14p by altering phospholipid metabolism so as to expand the pool of diacylglycerol (DAG) in the Golgi [4].
  • Yeast phosphatidylinositol transfer protein (Sec14p) is required for the production of secretory vesicles from the Golgi [4].
 

Chemical compound and disease context of SEC14

 

Biological context of SEC14

  • Nucleotide sequence analysis revealed the presence of an intron within the SEC14 structural gene, and predicted the synthesis of a hydrophilic polypeptide of 35 kD in molecular mass [6].
  • Gene disruption experiments indicated that SEC14 is an essential gene for yeast vegetative growth [6].
  • Alterations in the level of diacylglycerol consumption through alterations in phosphatidylcholine synthesis directly correlated with the level of SEC14-dependent invertase secretion and affected cell viability [7].
  • Administration of synthetic di8:0 diacylglycerol resulted in a partial rescue of cells from SEC14-mediated cell death [7].
  • Isolation and mapping of a human gene (SEC14L), partially homologous to yeast SEC14, that contains a variable number of tandem repeats (VNTR) site in its 3' untranslated region [8].
 

Anatomical context of SEC14

 

Associations of SEC14 with chemical compounds

  • Independent characterization of the SEC14 gene and the PIT1 gene, which encodes a phosphatidylinositol/phosphatidylcholine transfer protein in yeast, indicated that these two genes are identical [12].
  • In yeast, mutations in the CDP-choline pathway for phosphatidylcholine biosynthesis permit the cell to grow even when the SEC14 gene is completely deleted (Cleves, A., McGee, T., Whitters, E., Champion, K., Aitken, J., Dowhan, W., Goebl, M., and Bankaitis, V. (1991) Cell 64, 789-800) [13].
  • Regulation of phospholipid biosynthesis by phosphatidylinositol transfer protein Sec14p and its homologues. A critical role for phosphatidic acid [14].
  • PLD catalytic activity is necessary but not sufficient for 'bypass Sec14p', and yeast operating under 'bypass Sec14p' conditions are ethanol-sensitive [15].
  • Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: relationship to "bypass Sec14p" and inositol auxotrophy [16].
  • This regulation is uncoupled from PtdIns-transfer activity and argues for an interfacial presentation mode for Sec14-mediated potentiation of PtdIns kinases [17].
 

Other interactions of SEC14

  • Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth [18].
  • A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/phosphatidylcholine transfer protein, SEC14 [19].
  • These findings indicate that, first, PtdIns(4)P limitation is a major contributing factor to the secretory defect in sec14 cells; second, Sec14p function is coupled to the action of Pik1p, and; third, PtdIns(4)P has an important role in the Golgi-to-plasma membrane stage of secretion [10].
  • SUT1 constitutive expression in aerobiosis suppressed the ts phenotype of the sec14-1 mutation, restored growth of the sec14-null mutant and corrected the translocation defect of the vacuolar carboxypeptidase Y [20].
  • We show that Sfh1p, which shares 64% primary sequence identity with Sec14p, is nonfunctional as a Sec14p in vivo or in vitro [18].
 

Analytical, diagnostic and therapeutic context of SEC14

  • Northern blot analysis and PCR amplification of transcripts produced from the SEC14 gene demonstrated that two transcripts differing at their 3' ends were produced [21].
  • In confirmation, immunoprecipitation experiments demonstrated SEC14p to be an unglycosylated polypeptide, with an apparent molecular mass of some 37 kD, that behaved predominantly as a cytosolic protein in subcellular fractionation experiments [6].
  • Sequence analysis revealed that CaSec14p is a 301 amino acid protein, 67% identical to S. cerevisiae and Kluyveromyces iactis Sec14p, and 61% identical to the 300 amino-terminal residues of Yarrowia lipolytica Sec14p [22].
  • It is the purpose of the present study to examine by electron microscopy S. cerevisiae sec14 mutants and to compare the modifications along their secretory pathway with those occurring in a homologous mutant of Yarrowia lipolytica [23].
  • Crystallization of a phospholipid-bound Sec14p-like protein is a critical first step in obtaining the first high-resolution picture of how proteins of the Sec14p superfamily bind their phospholipid ligands [24].

References

  1. Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. Fang, M., Kearns, B.G., Gedvilaite, A., Kagiwada, S., Kearns, M., Fung, M.K., Bankaitis, V.A. EMBO J. (1996) [Pubmed]
  2. Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cleves, A.E., McGee, T.P., Whitters, E.A., Champion, K.M., Aitken, J.R., Dowhan, W., Goebl, M., Bankaitis, V.A. Cell (1991) [Pubmed]
  3. Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Sha, B., Phillips, S.E., Bankaitis, V.A., Luo, M. Nature (1998) [Pubmed]
  4. Essential role for diacylglycerol in protein transport from the yeast Golgi complex. Kearns, B.G., McGee, T.P., Mayinger, P., Gedvilaite, A., Phillips, S.E., Kagiwada, S., Bankaitis, V.A. Nature (1997) [Pubmed]
  5. Evidence for an intrinsic toxicity of phosphatidylcholine to Sec14p-dependent protein transport from the yeast Golgi complex. Xie, Z., Fang, M., Bankaitis, V.A. Mol. Biol. Cell (2001) [Pubmed]
  6. The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex. Bankaitis, V.A., Malehorn, D.E., Emr, S.D., Greene, R. J. Cell Biol. (1989) [Pubmed]
  7. Phosphatidylcholine synthesis influences the diacylglycerol homeostasis required for SEC14p-dependent Golgi function and cell growth. Henneberry, A.L., Lagace, T.A., Ridgway, N.D., McMaster, C.R. Mol. Biol. Cell (2001) [Pubmed]
  8. Isolation and mapping of a human gene (SEC14L), partially homologous to yeast SEC14, that contains a variable number of tandem repeats (VNTR) site in its 3' untranslated region. Chinen, K., Takahashi, E., Nakamura, Y. Cytogenet. Cell Genet. (1996) [Pubmed]
  9. Phospholipid transfer activity is relevant to but not sufficient for the essential function of the yeast SEC14 gene product. Skinner, H.B., Alb, J.G., Whitters, E.A., Helmkamp, G.M., Bankaitis, V.A. EMBO J. (1993) [Pubmed]
  10. Direct involvement of phosphatidylinositol 4-phosphate in secretion in the yeast Saccharomyces cerevisiae. Hama, H., Schnieders, E.A., Thorner, J., Takemoto, J.Y., DeWald, D.B. J. Biol. Chem. (1999) [Pubmed]
  11. Isolation of a cDNA from Arabidopsis thaliana that complements the sec14 mutant of yeast. Jouannic, N., Lepetit, M., Vergnolle, C., Cantrel, C., Gardies, A.M., Kader, J.C., Arondel, V. Eur. J. Biochem. (1998) [Pubmed]
  12. An essential role for a phospholipid transfer protein in yeast Golgi function. Bankaitis, V.A., Aitken, J.R., Cleves, A.E., Dowhan, W. Nature (1990) [Pubmed]
  13. Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turnover and INO1 regulation. Patton-Vogt, J.L., Griac, P., Sreenivas, A., Bruno, V., Dowd, S., Swede, M.J., Henry, S.A. J. Biol. Chem. (1997) [Pubmed]
  14. Regulation of phospholipid biosynthesis by phosphatidylinositol transfer protein Sec14p and its homologues. A critical role for phosphatidic acid. Holic, R., Zágorsek, M., Griac, P. Eur. J. Biochem. (2004) [Pubmed]
  15. Phospholipase D activity is required for suppression of yeast phosphatidylinositol transfer protein defects. Xie, Z., Fang, M., Rivas, M.P., Faulkner, A.J., Sternweis, P.C., Engebrecht, J.A., Bankaitis, V.A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  16. Pleiotropic alterations in lipid metabolism in yeast sac1 mutants: relationship to "bypass Sec14p" and inositol auxotrophy. Rivas, M.P., Kearns, B.G., Xie, Z., Guo, S., Sekar, M.C., Hosaka, K., Kagiwada, S., York, J.D., Bankaitis, V.A. Mol. Biol. Cell (1999) [Pubmed]
  17. Functional anatomy of phospholipid binding and regulation of phosphoinositide homeostasis by proteins of the sec14 superfamily. Schaaf, G., Ortlund, E.A., Tyeryar, K.R., Mousley, C.J., Ile, K.E., Garrett, T.A., Ren, J., Woolls, M.J., Raetz, C.R., Redinbo, M.R., Bankaitis, V.A. Mol. Cell (2008) [Pubmed]
  18. Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth. Li, X., Routt, S.M., Xie, Z., Cui, X., Fang, M., Kearns, M.A., Bard, M., Kirsch, D.R., Bankaitis, V.A. Mol. Biol. Cell (2000) [Pubmed]
  19. A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/phosphatidylcholine transfer protein, SEC14. Wu, W.I., Routt, S., Bankaitis, V.A., Voelker, D.R. J. Biol. Chem. (2000) [Pubmed]
  20. SUT1 suppresses sec14-1 through upregulation of CSR1 in Saccharomyces cerevisiae. Régnacq, M., Ferreira, T., Puard, J., Bergès, T. FEMS Microbiol. Lett. (2002) [Pubmed]
  21. Two transcripts, differing at their 3' ends, are produced from the Candida albicans SEC14 gene. Riggle, P.J., Slobodkin, I.V., Brown, D.H., Hanson, M.P., Volkert, T.L., Kumamoto, C.A. Microbiology (Reading, Engl.) (1997) [Pubmed]
  22. Cloning of Candida albicans SEC14 gene homologue coding for a putative essential function. Monteoliva, L., Sánchez, M., Pla, J., Gil, C., Nombela, C. Yeast (1996) [Pubmed]
  23. Transformations of membrane-bound organelles in sec 14 mutants of the yeasts Saccharomyces cerevisiae and Yarrowia lipolytica. Rambourg, A., Clermont, Y., Nicaud, J.M., Gaillardin, C., Kepes, F. Anat. Rec. (1996) [Pubmed]
  24. Crystallization and preliminary X-ray diffraction analysis of phospholipid-bound Sfh1p, a member of the Saccharomyces cerevisiae Sec14p-like phosphatidylinositol transfer protein family. Schaaf, G., Betts, L., Garrett, T.A., Raetz, C.R., Bankaitis, V.A. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
 
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