Rvs161p and Rvs167p, the Two Yeast Amphiphysin Homologs, Function Together in Vivo

Lombardi, Ruben; Riezman, Howard

doi:10.1074/jbc.m008735200

Cited by 57 publications

(71 citation statements)

References 31 publications

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“…Two other genes were UD R without being cdc13-1 suppressors: MAE1 and RVS161. RVS161 encodes an amphiphysin-like raft protein, which acts (with Rvs167) to regulate polarization of the actin cytoskeleton; thus its deletion has pleiotropic effects, which include disruption of endocytosis (Breton et al 2001;Lombardi and Riezman 2001). MAE1 encodes a mitochondrial malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate (Boles et al 1998).…”

Section: Discussionmentioning

confidence: 99%

A Genomewide Suppressor and Enhancer Analysis of cdc13-1 Reveals Varied Cellular Processes Influencing Telomere Capping in Saccharomyces cerevisiae

Addinall

Downey

et al. 2008

Genetics

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In Saccharomyces cerevisiae, Cdc13 binds telomeric DNA to recruit telomerase and to ''cap'' chromosome ends. In temperature-sensitive cdc13-1 mutants telomeric DNA is degraded and cell-cycle progression is inhibited. To identify novel proteins and pathways that cap telomeres, or that respond to uncapped telomeres, we combined cdc13-1 with the yeast gene deletion collection and used high-throughput spot-test assays to measure growth. We identified 369 gene deletions, in eight different phenotypic classes, that reproducibly demonstrated subtle genetic interactions with the cdc13-1 mutation. As expected, we identified DNA damage checkpoint, nonsense-mediated decay and telomerase components in our screen. However, we also identified genes affecting casein kinase II activity, cell polarity, mRNA degradation, mitochondrial function, phosphate transport, iron transport, protein degradation, and other functions. We also identified a number of genes of previously unknown function that we term RTC, for restriction of telomere capping, or MTC, for maintenance of telomere capping. It seems likely that many of the newly identified pathways/ processes that affect growth of budding yeast cdc13-1 mutants will play evolutionarily conserved roles at telomeres. The high-throughput spot-testing approach that we describe is generally applicable and could aid in understanding other aspects of eukaryotic cell biology.

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Section: Discussionmentioning

confidence: 99%

A Genomewide Suppressor and Enhancer Analysis of cdc13-1 Reveals Varied Cellular Processes Influencing Telomere Capping in Saccharomyces cerevisiae

Addinall

Downey

et al. 2008

Genetics

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“…This is not surprising, because cortical actin patches have recently been proven to be early endocytic structures (Kaksonen et al, 2003;Huckaba et al, 2004;Rodal et al, 2005). The significance of these interactions is bolstered by the fact that Rvs161p and Rvs167p dimerize and are partially redundant for function (Lombardi and Riezman, 2001), whereas Cap1p and Cap2p dimerize to form the ␣/␤ heterodimeric actin filament barbed-end capping protein (Amatruda et al, 1990). Furthermore, these genes display extensive physical and genetic interactions among themselves (Balakrishnan et al, 2005; Figure 6).…”

Section: Genetic Analysis Of Aip1p Mutantsmentioning

confidence: 99%

A Genetic Dissection of Aip1p's Interactions Leads to a Model for Aip1p-Cofilin Cooperative Activities

Clark

Teply

Haarer

et al. 2006

MBoC

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Actin interacting protein 1 (Aip1p) and cofilin cooperate to disassemble actin filaments in vitro and are thought to promote rapid turnover of actin networks in vivo. The precise method by which Aip1p participates in these activities has not been defined, although severing and barbed-end capping of actin filaments have been proposed. To better describe the mechanisms and biological consequences of Aip1p activities, we undertook an extensive mutagenesis of AIP1 aimed at disrupting and mapping Aip1p interactions. Site-directed mutagenesis suggested that Aip1p has two actin binding sites, the primary actin binding site lies on the edge of its N-terminal ␤-propeller and a secondary actin binding site lies in a comparable location on its C-terminal ␤-propeller. Random mutagenesis followed by screening for separation of function mutants led to the identification of several mutants specifically defective for interacting with cofilin but still able to interact with actin. These mutants suggested that cofilin binds across the cleft between the two propeller domains, leaving the actin binding sites exposed and flanking the cofilin binding site. Biochemical, genetic, and cell biological analyses confirmed that the actin binding-and cofilin binding-specific mutants are functionally defective, whereas the genetic analyses further suggested a role for Aip1p in an early, internalization step of endocytosis. A complementary, unbiased molecular modeling approach was used to derive putative structures for the Aip1p-cofilin complex, the most stable of which is completely consistent with the mutagenesis data. We theorize that Aip1p-severing activity may involve simultaneous binding to two actin subunits with cofilin wedged between the two actin binding sites of the N-and C-terminal propeller domains.

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“…Mutation of either one or both components of this heterodimer in yeast produces defects in endocytosis and actin function (11). Such a dual phenotype is typical of most mutations in actin regulatory and endocytosis genes in yeast (12).…”

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confidence: 99%

Tuba, a Novel Protein Containing Bin/Amphiphysin/Rvs and Dbl Homology Domains, Links Dynamin to Regulation of the Actin Cytoskeleton

Salazar

Kwiatkowski

Pellegrini

et al. 2003

Journal of Biological Chemistry

170

182

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Fission of clathrin-coated and other endocytic vesicles from the plasma membrane involves the cooperation of several membrane-associated proteins, among which the GTPase dynamin plays a key role (1, 2). The participation of dynamin in the fission of endocytic vesicles has been established by a variety of experimental approaches in Drosophila, cultured cells, and cell-free systems, although the precise mechanism of fission and the role of dynamin in this reaction remain unclear (3).Several dynamin partners thought to participate in dynamin recruitment or function have been identified (3,4). At the synapse, where endocytosis plays a key role in the recycling of synaptic vesicle membranes, two prominent dynamin partners are amphiphysin and endophilin (5-7). Amphiphysin has a three-domain structure with an evolutionarily conserved Nterminal module of ϳ250 amino acids called the Bin/amphiphysin/Rvs (BAR) 1 domain, a variable central region, and a Cterminal Src homology-3 (SH3) domain that binds dynamin. Endophilin has a similar domain structure (2). Although the N-terminal domain of endophilin is substantially divergent in amino acid composition from the BAR domain of amphiphysin, it shares some similarity at critical sites, leading to its classification as a BAR domain (8).2 Accordingly, the BAR domains of amphiphysin and endophilin share functional similarities because they both can bind and deform lipid bilayers and mediate homo-and heterodimerization (6, 8 -10). Dynamin also can bind and deform lipid bilayers, and it has been proposed that endophilin and amphiphysin might help to recruit and possibly assist dynamin in the generation of membrane curvature at endocytic pits (8, 10).The closest homologue of amphiphysin and endophilin in Saccharomyces cerevisiae is Rvs167, that forms a stable heterodimer with Rsv161; Rvs167 has a domain structure like amphiphysin, whereas Rvs161 (homologous to the mammalian protein Bin3) possesses only a BAR domain. Mutation of either one or both components of this heterodimer in yeast produces defects in endocytosis and actin function (11). Such a dual phenotype is typical of most mutations in actin regulatory and endocytosis genes in yeast (12). These observations, together with results from a variety of studies in mammalian cells, have suggested a link between endocytosis and actin, although such a link has remained mechanistically elusive (13,14). Foci of actin can often be seen at endocytic sites (15), and endocytic vesicles with actin tails have also been observed (16). Interest-* This work was supported in part by National Institutes of Health Grants NS36251 and CA46128 and United States Army Medical Research and Development Command Grant DAMD17-97-7068) (to P. D. C.); by National Institutes of Health Grant GM58801, a W. M. Keck Distinguished Young Scholar Award, and a McKnight Scholar Award (to F. B. G.); and by National Institutes of Health Grant GM62299 (to J. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article mu...

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Rvs161p and Rvs167p, the Two Yeast Amphiphysin Homologs, Function Together in Vivo

Cited by 57 publications

References 31 publications

A Genomewide Suppressor and Enhancer Analysis of cdc13-1 Reveals Varied Cellular Processes Influencing Telomere Capping in Saccharomyces cerevisiae

A Genomewide Suppressor and Enhancer Analysis of cdc13-1 Reveals Varied Cellular Processes Influencing Telomere Capping in Saccharomyces cerevisiae

A Genetic Dissection of Aip1p's Interactions Leads to a Model for Aip1p-Cofilin Cooperative Activities

Tuba, a Novel Protein Containing Bin/Amphiphysin/Rvs and Dbl Homology Domains, Links Dynamin to Regulation of the Actin Cytoskeleton

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