The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity

Breton, Annick M.; Schaeffer, Jacques; Aigle, Michel

doi:10.1002/yea.755.abs

Cited by 7 publications

(10 citation statements)

References 46 publications

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“…Hence, dAmph could also be involved in exocytotic vesicle trafficking to target secretory vesicles to the T‐tubule membrane, and thus participate in T‐tubule membrane construction or maintenance. A precedent for such a function in cell membrane integrity has been recently demonstrated for the yeast Rvsps (62,63).…”

Section: Amphiphysin Flexes Musclesmentioning

confidence: 99%

Amphiphysins: Raising the BAR for Synaptic Vesicle Recycling and Membrane Dynamics

Zhang

Zelhof

2002

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Amphiphysins, members of the BAR (Bin-Amphiphysin-Rvsp) protein super family, have been postulated to play a key role in clathrin-mediated endocytosis of synaptic vesicles (SVs). This review focuses on recent genetic studies of the role of amphiphysins in SV recycling and membrane morphogenesis. In the mouse, brain-specific amphiphysin I and II regulate, but are not essential for, SV recycling. The role of this regulation appears important, as mice deficient in these proteins have seizures and are deficient in learning and memory. In the fruit fly Drosophila melanogaster, amphiphysin is found in muscles and is enriched at postsynaptic membranes of neuromuscular junctions (NMJs); however, it does not play a role in SV recycling. Rather, amphiphysin in fly muscles appears to regulate the organization and structure of the muscle T-tubule system and possibly the subsynaptic reticulum. Amphiphysin is also involved in membrane organization in both neurons and non-neuronal cells in Drosophila. These studies reveal pleiotropic functions for amphiphysins in clathrin-mediated endocytosis and the regulation of membrane dynamics, perhaps through the actin cytoskeleton.

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Section: Amphiphysin Flexes Musclesmentioning

confidence: 99%

Amphiphysins: Raising the BAR for Synaptic Vesicle Recycling and Membrane Dynamics

Zhang

Zelhof

2002

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“…RVS167 is not an essential gene, although it is required for viability under certain growth conditions (Bauer et al, 1993;Colwill et al, 1999) and in strains deleted for a number of other actin cytoskeleton genes (Lila and Drubin, 1997;Singer-Krü ger and Ferro-Novick, 1997;Breton and Aigle, 1998;Breton et al, 2001). RVS167 is not an essential gene, although it is required for viability under certain growth conditions (Bauer et al, 1993;Colwill et al, 1999) and in strains deleted for a number of other actin cytoskeleton genes (Lila and Drubin, 1997;Singer-Krü ger and Ferro-Novick, 1997;Breton and Aigle, 1998;Breton et al, 2001).…”

Section: Phosphorylation Of Rvs167p In Yeastmentioning

confidence: 99%

“…Deletion of RVS167 or RVS161 causes a phenotype consistent with a role for the Rvs proteins in cortical actin cytoskeleton organization, endocytosis, and membrane dynamics. Ultrastructural studies have revealed that rvs167 mutants accumulate late secretory vesicles at sites of membrane and cell wall construction (Breton et al, 2001). Ultrastructural studies have revealed that rvs167 mutants accumulate late secretory vesicles at sites of membrane and cell wall construction (Breton et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Regulation of the Yeast Amphiphysin Homologue Rvs167p by Phosphorylation

Friesen

Murphy

Breitkreutz

et al. 2003

MBoC

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The yeast amphiphysin homologue Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. Rvs167p is a phosphoprotein in vegetatively growing cells and shows increased phosphorylation upon treatment with mating pheromone. Previous work has shown that Rvs167p can be phosphorylated in vitro by the cyclin-dependent kinase Pho85p complexed with its cyclin Pcl2p. Using chymotryptic phosphopeptide mapping, we have identified the sites on which Rvs167p is phosphorylated in vitro by Pcl2p-Pho85p. We have shown that these same sites are phosphorylated in vivo during vegetative growth and that phosphorylation at two of these sites is Pcl-Pho85p dependent. In cells treated with mating pheromone, the MAP kinase Fus3p is needed for full phosphorylation of Rvs167p. Functional genomics and genetics experiments revealed that mutation of other actin cytoskeleton genes compromises growth of a strain in which phosphorylation of Rvs167p is blocked by mutation. Phosphorylation of Rvs167p inhibits its interaction in vitro with Las17p, an activator of the Arp2/3 complex, as well as with a novel protein, Ymr192p. Our results suggest that phosphorylation of Rvs167p by a cyclin-dependent kinase and by a MAP kinase is an important mechanism for regulating protein complexes involved in actin cytoskeleton function.

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“…Rvs167p contains other domains and interacts with many proteins that have well‐characterized roles in the actin cytoskeleton organization, including Abp1p, Acf2p, Act1p, Las17p, Sla1p, Sla2p, and Srv2p (Ren et al , 2006). In addition, RVS167 shows synthetic lethal or synergistic negative growth interactions with MYO1 , MYO2 , and ACT1 as well as with SLT2 and KRE6 (Breton et al , 2001). Rvs161p is required for actin repolarization upon salt stress and is associated with lipid rafts (Balguerie et al , 2002).…”

Section: Introductionmentioning

confidence: 99%

Hob3p, the fission yeast ortholog of human BIN3, localizes Cdc42p to the division site and regulates cytokinesis

Coll

Rincón

Izquierdo

et al. 2007

EMBO J

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Cdc42 GTPase is required for polarization in eukaryotic cells, but its spatial regulation is poorly understood. In Schizosaccharomyces pombe, Cdc42p is activated by Scd1p and Gef1p, two guanine‐nucleotide exchange factors. Two‐hybrid screening identified Hob3p as a Gef1p binding partner. Hob3p is a BAR domain‐containing protein ortholog of human Bin3. Hob3p also interacts directly with Cdc42p independently of Gef1p. Hob3p, Cdc42p and Gef1p form a complex, and Hob3p facilitates Gef1p–Cdc42p interaction and activation. Hob3p forms a ring in the division area, similar to that of Gef1p. This localization requires actin polymerization and Cdc15p but is independent of the septation initiation network. Hob3p is required for the concentration of Cdc42p to the division area. The actomyosin ring contraction is slower in hob3Δ than in wild‐type cells, and this contributes to its cytokinesis defect. Moreover, this report extends previous evidence that human Bin3 suppresses the cytokinesis phenotype of hob3Δ cells, showing that Bin3 can partially recover the GTP‐Cdc42p level and its localization. These results suggest that Hob3p is required to recruit and activate Cdc42p at the cell division site and that this function might be conserved in other eukaryotes.

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The yeast Rvs161 and Rvs167 proteins are involved in secretory vesicles targeting the plasma membrane and in cell integrity

Cited by 7 publications

References 46 publications

Amphiphysins: Raising the BAR for Synaptic Vesicle Recycling and Membrane Dynamics

Amphiphysins: Raising the BAR for Synaptic Vesicle Recycling and Membrane Dynamics

Regulation of the Yeast Amphiphysin Homologue Rvs167p by Phosphorylation

Hob3p, the fission yeast ortholog of human BIN3, localizes Cdc42p to the division site and regulates cytokinesis

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