Research Topics
Genomes and Genes | J E GerstSummaryAffiliation: Weizmann Institute of Science Country: Israel Publications
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Detail Information
Publications
SNAREs and SNARE regulators in membrane fusion and exocytosisJ E Gerst
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel
Cell Mol Life Sci 55:707-34. 1999..g. 'SNARE-masters') in mediating events leading to membrane fusion. A model to illustrate the dynamic cycling of SNAREs between fusion-incompetent and fusion-competent states, called the SNARE cycle, is presented...
Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic functionJ E Gerst
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
J Biol Chem 272:16591-8. 1997....
Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosisV Lustgarten
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
Mol Cell Biol 19:4480-94. 1999..Moreover, this regulation appears specific to one of two parallel exocytic paths which are operant in yeast cells...
t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeastM Marash
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
EMBO J 20:411-21. 2001..Thus, modulation of t-SNARE phosphorylation regulates SNARE complex assembly and membrane fusion in vivo...
Yeast exocytic v-SNAREs confer endocytosisS Gurunathan
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
Mol Biol Cell 11:3629-43. 2000..Thus, we propose that synaptobrevin/VAMP family members are engaged in anterograde and retrograde protein sorting steps between the Golgi and the plasma membrane...
Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeastD David
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel
J Cell Biol 143:1167-82. 1998....
Identification and characterization of a gene encoding phospholipase D activity in yeastM Waksman
Department of Biological Regulation, Weizmann Institute of Science, Rehovot, Israel
J Biol Chem 271:2361-4. 1996..Because the biological role of PLD is not well understood, we expect that delta pld1 yeast will become a useful tool for the characterization of PLD functions as well as for the identification of mammalian PLD homologs...
Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiaeV Protopopov
Department of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, New York 10029 6574
Cell 74:855-61. 1993..Our findings clearly place the Snc proteins on the late secretory pathway in S. cerevisiae and provide direct in vivo evidence that synaptobrevin-like proteins mediate the targeting and transport of secretory proteins...
Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteinsA Couve
J Biol Chem 269:23391-4. 1994..We suggest, then, that recognition of the plasma membrane by secretory vesicles may involve the formation of a Snc-Sec9 complex and that this interaction has evolved as a fundamental step in secretory processes...
SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: genetic interactions with the RAS and CAP genesJ E Gerst
Department of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, NY 10029 6574
Proc Natl Acad Sci U S A 89:4338-42. 1992..Multicopy plasmids expressing SNC1 suppress only the loss of the C-terminal functions of CAP and only in the presence of activated RAS2...
Two separate functions are encoded by the carboxyl-terminal domains of the yeast cyclase-associated protein and its mammalian homologs. Dimerization and actin bindingA Zelicof
Department of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, New York 10029, USA
J Biol Chem 271:18243-52. 1996..Finally, we present evidence that links a segment of the proline-rich region of CAP to its localization in yeast. Together, these results suggest that all three domains of CAP proteins are functional...
Molecular cloning and characterization of a rat homolog of CAP, the adenylyl cyclase-associated protein from Saccharomyces cerevisiaeA Zelicof
Department of Cell Biology and Anatomy, Mount Sinai School of Medicine, New York, New York 10029 6574
J Biol Chem 268:13448-53. 1993..Matviw, H., Yu, G., and Young, D. (1992) Mol. Cell. Biol. 12, 5033-5040), demonstrates that both cyclase-associated proteins and their functions may have evolved with mammalian cells...
