Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis

Patrick Brennwald, Brian Kearns, Kathy Champion, Sirkka Keränen, Vytas Bankaitis, Peter Novick

Research output: Contribution to journalArticleScientificpeer-review

298 Citations (Scopus)

Abstract

To identify potential Sec4 effectors, we isolated high copy suppressors of a Sec4 effector domain mutant. The most potent of these was found to be SEC9, a gene required for post-Golgi transport. The sole essential domain of Sec9 has significant sequence similarity to the neuronal protein SNAP-25, a component of the SNARE complex, that is implicated in vesicle targeting and fusion. Analogous to SNAP-25, Sec9 is bound to the yeast plasma membrane and is absent from post-Golgi vesicles. Furthermore, Sec9 is physically associated with two proteins that are homologous to components of the neuronal SNARE complex. Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases.
Original languageEnglish
Pages (from-to)245-258
JournalCell
Volume79
Issue number2
DOIs
Publication statusPublished - 21 Oct 1994
MoE publication typeA1 Journal article-refereed

Fingerprint

SNARE Proteins
Exocytosis
Yeast
Yeasts
Synaptosomal-Associated Protein 25
rab GTP-Binding Proteins
GTP Phosphohydrolases
Cell membranes
Fusion reactions
Genes
Cell Membrane
Proteins

Keywords

  • Sec9
  • SNAP-25
  • Sec-4

Cite this

Brennwald, P., Kearns, B., Champion, K., Keränen, S., Bankaitis, V., & Novick, P. (1994). Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell, 79(2), 245-258. https://doi.org/10.1016/0092-8674(94)90194-5
Brennwald, Patrick ; Kearns, Brian ; Champion, Kathy ; Keränen, Sirkka ; Bankaitis, Vytas ; Novick, Peter. / Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. In: Cell. 1994 ; Vol. 79, No. 2. pp. 245-258.
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title = "Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis",
abstract = "To identify potential Sec4 effectors, we isolated high copy suppressors of a Sec4 effector domain mutant. The most potent of these was found to be SEC9, a gene required for post-Golgi transport. The sole essential domain of Sec9 has significant sequence similarity to the neuronal protein SNAP-25, a component of the SNARE complex, that is implicated in vesicle targeting and fusion. Analogous to SNAP-25, Sec9 is bound to the yeast plasma membrane and is absent from post-Golgi vesicles. Furthermore, Sec9 is physically associated with two proteins that are homologous to components of the neuronal SNARE complex. Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases.",
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Brennwald, P, Kearns, B, Champion, K, Keränen, S, Bankaitis, V & Novick, P 1994, 'Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis', Cell, vol. 79, no. 2, pp. 245-258. https://doi.org/10.1016/0092-8674(94)90194-5

Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. / Brennwald, Patrick; Kearns, Brian; Champion, Kathy; Keränen, Sirkka; Bankaitis, Vytas; Novick, Peter.

In: Cell, Vol. 79, No. 2, 21.10.1994, p. 245-258.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Brennwald, Patrick

AU - Kearns, Brian

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AU - Bankaitis, Vytas

AU - Novick, Peter

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AB - To identify potential Sec4 effectors, we isolated high copy suppressors of a Sec4 effector domain mutant. The most potent of these was found to be SEC9, a gene required for post-Golgi transport. The sole essential domain of Sec9 has significant sequence similarity to the neuronal protein SNAP-25, a component of the SNARE complex, that is implicated in vesicle targeting and fusion. Analogous to SNAP-25, Sec9 is bound to the yeast plasma membrane and is absent from post-Golgi vesicles. Furthermore, Sec9 is physically associated with two proteins that are homologous to components of the neuronal SNARE complex. Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases.

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