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

doi: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

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

VTT Technical Research Centre of Finland

Research output: Contribution to journal › Article › Scientific › peer-review

324 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 language	English
Pages (from-to)	245-258
Journal	Cell
Volume	79
Issue number	2
DOIs	https://doi.org/10.1016/0092-8674(94)90194-5
Publication status	Published - 21 Oct 1994
MoE publication type	A1 Journal article-refereed

Keywords

Sec9
SNAP-25
Sec-4

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10.1016/0092-8674(94)90194-5

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@article{eb1a5350b39c4c4abfb1f12c140e4735,

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.",

keywords = "Sec9, SNAP-25, Sec-4",

author = "Patrick Brennwald and Brian Kearns and Kathy Champion and Sirkka Ker{\"a}nen and Vytas Bankaitis and Peter Novick",

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T1 - Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis

AU - Brennwald, Patrick

AU - Kearns, Brian

AU - Champion, Kathy

AU - Keränen, Sirkka

AU - Bankaitis, Vytas

AU - Novick, Peter

N1 - Project code: BEL4301

PY - 1994/10/21

Y1 - 1994/10/21

N2 - 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.

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.

KW - Sec9

KW - SNAP-25

KW - Sec-4

U2 - 10.1016/0092-8674(94)90194-5

DO - 10.1016/0092-8674(94)90194-5

M3 - Article

SN - 0092-8674

VL - 79

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EP - 258

JO - Cell

JF - Cell

IS - 2

ER -

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

Abstract

Keywords

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