Cloning and sequencing of the yeast <i>Saccharomyces cerevisiae SEC1</i> gene localized on chromosome IV

Aalto, Markku K.; Ruohonen, Laura; Hosono, Kuniaki; Keränen, Sirkka

doi:10.1002/yea.320070613

Cited by 71 publications

(43 citation statements)

References 31 publications

(21 reference statements)

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“…By definition, these regulators are expected to associate directly with specific v-or t-SNAREs and act to downregulate trafficking functions by modulating their entry into SNARE complexes. Thus, dissociation of SNARE regulators from SNAREs, or their inactivation, is expected to precede complex assembly and membrane fusion.A conserved family of SNARE regulators which function in constitutive and regulated secretory systems is that of yeast Sec1 and its homologs found in higher organisms (1,23,26,34,47,55). SEC1 was identified in the original sec mutant screen (45) and encodes a soluble protein that interacts with members of the Sso/syntaxin family of t-SNAREs (2,23,47,48).…”

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confidence: 99%

Yeast VSM1 Encodes a v-SNARE Binding Protein That May Act as a Negative Regulator of Constitutive Exocytosis

Lustgarten

Gerst

1999

Molecular and Cellular Biology

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We have screened for proteins that interact with v-SNAREs of the late secretory pathway in the yeast Saccharomyces cerevisiae. A novel protein, designated Vsm1, binds tightly to the Snc2 v-SNARE in the two-hybrid system and can be coimmunoprecipitated with Snc1 or Snc2 from solubilized yeast cell extracts. Disruption of the VSM1 gene results in an increase of proteins secreted into the medium but does not affect the processing or secretion of invertase. In contrast, VSM1 overexpression in cells which bear a temperature-sensitive mutation in the Sec9 t-SNARE (sec9-4 cells) results in the accumulation of non-invertase-containing lowdensity secretory vesicles, inhibits cell growth and the secretion of proteins into the medium, and blocks rescue of the temperature-sensitive phenotype by SNC1 overexpression. Yet, VSM1 overexpression does not affect yeast bearing a sec9-7 allele which, in contrast to sec9-4, encodes a t-SNARE protein capable of forming a stable SNARE complex in vitro at restrictive temperatures. On the basis of these results, we propose that Vsm1 is a novel v-SNARE-interacting protein that appears to act as negative regulator of constitutive exocytosis. Moreover, this regulation appears specific to one of two parallel exocytic paths which are operant in yeast cells.SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein [SNAP] receptor) proteins comprise distinct families of membrane-associated receptors that are components of the vesicle docking and fusion machinery in eukaryotes (62; reviewed in references 35 and 54). Evidence from evolutionarily divergent systems, e.g., from yeast to mammals, suggests that the role of SNAREs in protein transport is highly conserved (reviewed in references 7 and 21). SNAREs act throughout the secretory pathway to confer the trafficking of cargo-containing carrier vesicles and may also participate in compartmental organization. SNAREs found on vesicular compartments (v-SNAREs) are proposed to interact with specific cognate receptors (t-SNAREs) present on target compartments to form a prefusion SNARE complex. Thus, v-SNAREt-SNARE (v-t SNARE) assembly confers vesicle docking; one of the first events leading to membrane fusion. Moreover, recent work has suggested that together v-and t-SNAREs may provide the minimal requirements necessary for conferring both membrane association and bilayer fusion, using a liposome-based in vitro assay (70). However, there is still some controversy surrounding the role of SNAREs in the fusion event itself (13, 65).To confer specificity to protein transport, SNARE assembly leading to membrane fusion is expected to occur only on appropriate target membranes. Yet, the v-and t-SNAREs involved in Golgi and post-Golgi trafficking events passage through the early secretory pathway and are likely to reside together on identical endoplasmic reticulum (ER)-and Golgiderived transport vesicles. Therefore, some mechanism(s) should prevent nonproductive SNARE partnering from occurring between opposing membranes early in the pathway. Likewi...

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confidence: 99%

Yeast VSM1 Encodes a v-SNARE Binding Protein That May Act as a Negative Regulator of Constitutive Exocytosis

Lustgarten

Gerst

1999

Molecular and Cellular Biology

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“…Several regulatory proteins that interact with SNAREs have been reported. Sec1p in yeast and its homologues nSec1p, Munc18, and unc18 in higher eukaryotes have been shown to regulate exocytosis (53)(54)(55)(56)(57)(58). This protein family acts directly on the syntaxin t-SNAREs (54, 59 -61).…”

Section: Mutantmentioning

confidence: 99%

Aut7p, a Soluble Autophagic Factor, Participates in Multiple Membrane Trafficking Processes

Legesse‐Miller

Sagiv

Glozman

et al. 2000

Journal of Biological Chemistry

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“…They are thought to interact via the coiled-coil domains predicted from their sequences (Chapman et al, 1994;Hayashi et al, 1994). Assembly of the SNARE complex is regulated by the Secl/Slyl family of proteins (Aalto et al, 1991;Dascher et al, 1991;Ossig et al, 1991;Aalto et al, 1992;Pevsner, 1996) and the Ypt/Rab family of small GTPbinding proteins (Salminen and Novick, 1987;Segev et al, 1988;Novick and Brennwald, 1993;Pfeffer, 1994). The cognate SNARE complex acts as a scaffold for the binding of the ATPase NSF via the soluble NSF attachment proteins (SNAPs) (Sollner et al, 1993b).…”

Section: Introductionmentioning

confidence: 99%

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

Hui

Nakamura

Sonnichsen

et al. 1997

MBoC

124

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The early Golgi t-SNARE (target-membrane-associated soluble-N-ethylmaleimide-sensitive factor attachment protein receptor) syntaxin 5 is thought to specify the docking site for both COPI and COPII coated vesicles originating from the endoplasmic reticulum (ER) and COPI vesicles on the retrograde pathway. We now show that there are two forms of syntaxin 5 that appear to be generated from the same mRNA by alternative initiation of translation. The short form (35 kDa) corresponds to the published sequence. The long form (42 kDa) has an N-terminal cytoplasmic extension containing a predicted type II ER retrieval signal. When grafted onto a reporter molecule, this signal localized the construct to the ER. Biochemical fractionation and immunofluorescence microscopy showed that there was less of the long form in the Golgi apparatus and more in peripheral punctate structures, some of which colocalized with markers of the intermediate compartment. The predicted absence of the long form in budding yeast points to a function unique to higher organisms.

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Cloning and sequencing of the yeast Saccharomyces cerevisiae SEC1 gene localized on chromosome IV

Cited by 71 publications

References 31 publications

Yeast VSM1 Encodes a v-SNARE Binding Protein That May Act as a Negative Regulator of Constitutive Exocytosis

Yeast VSM1 Encodes a v-SNARE Binding Protein That May Act as a Negative Regulator of Constitutive Exocytosis

Aut7p, a Soluble Autophagic Factor, Participates in Multiple Membrane Trafficking Processes

An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal.

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