Gyp5p and Gyl1p are involved in the control of polarized exocytosis in budding yeast

Chesneau, Laurent; Dupré-Crochet, Sophie; Burdina, Anna O.; Roger, Jérôme E.; Panse, Sophie Le; Jacquet, Michel; Cuif, Marie-Hélène

doi:10.1242/jcs.01349

Cited by 22 publications

(37 citation statements)

References 40 publications

(39 reference statements)

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“…In this way, overexpression of Gyp5p and Gyl1p mimics loss of Rvs167p (84). Another study, however, found that Gyp5p and Gyl1p function in post-Golgi apparatus traffic (see above) (33). Perhaps Gyp5p and Gyl1p function in early steps of the secretory pathway with Ypt1p and in late steps of the secretory pathway with Sec4p.…”

Section: Roles Of Rvs161p and Rvs167p In The Secretory Pathwaymentioning

confidence: 94%

“…Loss of Gyp1p and Gyl1p, either singly or in combination, did not result in Rvs phenotypes with the possible exception of bipolar bud site selection. Furthermore, overexpression of Gyp5p and Gyl1p did not perturb actin patch polarization or endocytosis, so the inhibitory effect seems to be restricted to ER-to-Golgi apparatus transport (33,84,317).…”

Section: Roles Of Rvs161p and Rvs167p In The Secretory Pathwaymentioning

confidence: 95%

“…gyp5⌬ interacts genetically with sec2 mutations affecting the Sec4p GEF. At low temperature, gyp5⌬ gyl1⌬ double mutant cells exhibit a slight defect in growth and polarized secretion and accumulate secretory vesicles at sites of polarized growth (33).…”

Section: Roles Of Rvs161p and Rvs167p In The Secretory Pathwaymentioning

confidence: 99%

“…It may be relevant that a human gene mutated in a mental retardation disorder encodes a neuronal Rab GDP dissociation inhibitor (44). In yeast, Rvs167p interacts with a catalytically active Rab-GAP (Gyp5p) as well as a catalytically inactive Rab-GAP family member (Gyl1p) (33,84,317), rvs167 genetically interacts with a gene encoding an endosomal Rab protein (Ypt51p/Vps21p) (296), and loss of Rvs161p or Rvs167p cause accumulation of what appear to be exocytic vesicles that likely carry the Rab protein Ypt1p (20).…”

Section: Amphiphysin 1 Knockout Micementioning

confidence: 99%

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The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Ren

Vajjhala

Lee

et al. 2006

Microbiol Mol Biol Rev

192

186

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SUMMARY The Bin1/amphiphysin/Rvs167 (BAR) domain proteins are a ubiquitous protein family. Genes encoding members of this family have not yet been found in the genomes of prokaryotes, but within eukaryotes, BAR domain proteins are found universally from unicellular eukaryotes such as yeast through to plants, insects, and vertebrates. BAR domain proteins share an N-terminal BAR domain with a high propensity to adopt α-helical structure and engage in coiled-coil interactions with other proteins. BAR domain proteins are implicated in processes as fundamental and diverse as fission of synaptic vesicles, cell polarity, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, signal transduction, apoptosis, secretory vesicle fusion, excitation-contraction coupling, learning and memory, tissue differentiation, ion flux across membranes, and tumor suppression. What has been lacking is a molecular understanding of the role of the BAR domain protein in each process. The three-dimensional structure of the BAR domain has now been determined and valuable insight has been gained in understanding the interactions of BAR domains with membranes. The cellular roles of BAR domain proteins, characterized over the past decade in cells as distinct as yeasts, neurons, and myocytes, can now be understood in terms of a fundamental molecular function of all BAR domain proteins: to sense membrane curvature, to bind GTPases, and to mold a diversity of cellular membranes.

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Section: Roles Of Rvs161p and Rvs167p In The Secretory Pathwaymentioning

confidence: 94%

Section: Roles Of Rvs161p and Rvs167p In The Secretory Pathwaymentioning

confidence: 95%

Section: Roles Of Rvs161p and Rvs167p In The Secretory Pathwaymentioning

confidence: 99%

Section: Amphiphysin 1 Knockout Micementioning

confidence: 99%

See 2 more Smart Citations

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Ren

Vajjhala

Lee

et al. 2006

Microbiol Mol Biol Rev

192

186

View full text Add to dashboard Cite

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“…We have found that the rvs delete strains have synthetic growth defects in combination with two genes involved in vesicle trafficking from endoplasmic reticulum (ER) to Golgi, sec22⌬ and rud3⌬ (Newman and Ferro-Novick, 1990;Kim, 2003), suggesting that the Rvs proteins may be required for proper ER-to-Golgi trafficking. Additional evidence to support a role for Rvs167p in ER-to-Golgi vesicle trafficking comes from screens for proteins that interact with the SH3 domain of Rvs167p: the Rvs167p SH3 domain has been shown to bind to at least one protein involved in vesicle trafficking from ER to Golgi: Gyp5p (Bon et al, 2000;Ho et al, 2002;Chesneau et al, 2004;Friesen et al, 2005) as well as the Gyp5p-interacting protein Gyl1p (Chesneau et al, 2004;Friesen et al, 2005). In addition, the finding that RVS167 and RVS161 have synthetic genetic interactions with VPS21, a gene involved in the delivery of vacuolar and endocytosed proteins to the vacuole (Gerrard et al, 2000; interaction with RVS167 reported previously by SingerKrü ger and Ferro-Novick, 1997) suggests a role for Rvs161p-167p in multiple vesicle-mediated functions.…”

Section: Vesicle Traffickingmentioning

confidence: 99%

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals Roles for the Rvs Heterodimer In Vivo

Friesen

Humphries

et al. 2006

MBoC

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We have used comprehensive synthetic lethal screens and biochemical assays to examine the biological role of the yeast amphiphysin homologues Rvs161p and Rvs167p, two proteins that play a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. We found that unlike some forms of amphiphysin, Rvs161p-Rvs167p acts as an obligate heterodimer during vegetative growth and neither Rvs161p nor Rvs167p forms a homodimer in vivo. RVS161 and RVS167 have an identical set of 49 synthetic lethal interactions, revealing functions for the Rvs proteins in cell polarity, cell wall synthesis, and vesicle trafficking as well as a shared role in mating. Consistent with these roles, we show that the Rvs167p-Rvs161p heterodimer, like its amphiphysin homologues, can bind to phospholipid membranes in vitro, suggesting a role in vesicle formation and/or fusion. Our genetic screens also reveal that the interaction between Abp1p and the Rvs167p Src homology 3 (SH3) domain may be important under certain conditions, providing the first genetic evidence for a role for the SH3 domain of Rvs167p. Our studies implicate heterodimerization of amphiphysin family proteins in various functions related to cell polarity, cell integrity, and vesicle trafficking during vegetative growth and the mating response. INTRODUCTIONRVS161 and RVS167, which encode closely related proteins in Saccharomyces cerevisiae, were first identified in a screen for mutants that exhibited reduced viability upon starvation (Bauer et al., 1993). Mutation of RVS161 or RVS167 causes a phenotype consistent with a role for the Rvs proteins in cortical actin cytoskeleton organization and endocytosis: loss of viability and unusual cell morphology in poor growth medium or salt-containing medium, delocalized actin distribution under suboptimal growth conditions, abnormal (random) budding in diploids, and defects in endocytosis and sporulation (Bauer et al., 1993). Ultrastructural studies have revealed that rvs mutants accumulate late secretory vesicles at sites of membrane and cell wall construction (Breton et al., 2001), suggesting an additional role for Rvs161p and Rvs167p in vesicle trafficking.Rvs161p and Rvs167p are members of the BAR-domain family of proteins, which includes Bin1, Amphiphysin, and Rvs proteins (Sivadon et al., 1997). Amphiphysins are enriched in the mammalian brain and seem to function in synaptic vesicle endocytosis (for review, see Zhang and Zelhof, 2002). Bin1 is a splice isoform of amphiphysin 2 that has features of a tumor suppressor (Sakamuro et al., 1996). Proteins in this family are characterized by the presence of a conserved BAR domain, and it is through their BAR domains that Rvs161p interacts with Rvs167p (Navarro et al., 1997;Sivadon et al., 1997;Colwill et al., 1999). The crystal structure of the BAR domain of Drosophila amphiphysin has recently been solved (Peter et al., 2004). It is a crescentshaped dimer, in which each monomer forms a coiled coil. The curved shape is only revealed upon dimerization of the two slightly kinked ...

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Current awareness on yeast

2005

Yeast

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In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Books, Reviews & Symposia; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (5 weeks journals ‐ search completed 12th. Jan. 2005)

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Gyp5p and Gyl1p are involved in the control of polarized exocytosis in budding yeast

Cited by 22 publications

References 40 publications

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy

Characterization of the Yeast Amphiphysins Rvs161p and Rvs167p Reveals Roles for the Rvs Heterodimer In Vivo

Current awareness on yeast

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