Verprolin: A cool set of actin‐binding sites and some very HOT prolines

Munn, Alan Leslie; Thanabalu, Thirumaran

doi:10.1002/iub.195

Cited by 9 publications

(7 citation statements)

References 32 publications

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“…Interestingly, an actin filament stabilizing form of actin encoded by the act1-159 allele (Belmont and Drubin 1998) has little-to-no ability to suppress vrp1∆ (Figure 2; act1-159 is carried on plasmid pBH662). Verprolin is reported to be an actin monomer binding protein that also interacts with the Arp2/3 activator Las17 (WASP) and the cytokinesis regulator Hof1p (Munn and Thanabalu 2009). Verprolin acts as an actin monomer chaperone for actin filament assembly (Munn and Thanabalu 2009), and we propose that loss of verprolin can be suppressed by increasing the amount of monomeric actin but not filamentous actin.…”

Section: Resultsmentioning

confidence: 99%

“…Verprolin is reported to be an actin monomer binding protein that also interacts with the Arp2/3 activator Las17 (WASP) and the cytokinesis regulator Hof1p (Munn and Thanabalu 2009). Verprolin acts as an actin monomer chaperone for actin filament assembly (Munn and Thanabalu 2009), and we propose that loss of verprolin can be suppressed by increasing the amount of monomeric actin but not filamentous actin.…”

Section: Resultsmentioning

confidence: 99%

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Actin Dosage Lethality Screening in Yeast Mediated by Selective Ploidy Ablation Reveals Links to Urmylation/Wobble Codon Recognition and Chromosome Stability

Haarer

Mi-Mi

Cho

et al. 2013

G3 Genes|Genomes|Genetics

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The actin cytoskeleton exists in a dynamic equilibrium with monomeric and filamentous states of its subunit protein actin. The spatial and temporal regulation of actin dynamics is critical to the many functions of actin. Actin levels are remarkably constant, suggesting that cells have evolved to function within a narrow range of actin concentrations. Here we report the results of screens in which we have increased actin levels in strains deleted for the ~4800 nonessential yeast genes using a technical advance called selective ploidy ablation. We detected 83 synthetic dosage interactions with actin, 78 resulted in reduced growth, whereas in 5 cases overexpression of actin suppressed the growth defects caused by the deleted genes. The genes were highly enriched in several classes, including transfer RNA wobble uridine modification, chromosome stability and segregation, cell growth, and cell division. We show that actin overexpression sequesters a limited pool of eEF1A, a bifunctional protein involved in aminoacyl-transfer RNA recruitment to the ribosome and actin filament cross-linking. Surprisingly, the largest class of genes is involved in chromosome stability and segregation. We show that actin mutants have chromosome segregation defects, suggesting a possible role in chromosome structure and function. Monomeric actin is a core component of the INO80 and SWR chromatin remodeling complexes and the NuA4 histone modification complex, and our results suggest these complexes may be sensitive to actin stoichiometry. We propose that the resulting effects on chromatin structure can lead to synergistic effects on chromosome stability in strains lacking genes important for chromosome maintenance.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Actin Dosage Lethality Screening in Yeast Mediated by Selective Ploidy Ablation Reveals Links to Urmylation/Wobble Codon Recognition and Chromosome Stability

Haarer

Mi-Mi

Cho

et al. 2013

G3 Genes|Genomes|Genetics

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“…Myo5 was shown to be present in a subset of cortical actin-patchlike structures, which were already suspected to correspond to the sites of endocytosis [21,22]. Recruitment of Myo5 to the cortical actin patches is at least partially dependent on the interaction of its SH3 domain with the yeast homologue of human WIP (Wiskott-Aldrich interacting protein) Vrp1 [20], a protein that bears several G-actinbinding sites [23].…”

Section: The Yeast Myosins-i Are Transiently Recruited To the Sites Omentioning

confidence: 99%

Function and regulation of Saccharomyces cerevisiae myosins-I in endocytic budding

Giblin

Fernández-Golbano

Idrissi

et al. 2011

Biochemical Society Transactions

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Myosins-I are widely expressed actin-dependent motors which bear a phospholipid-binding domain. In addition, some members of the family can trigger Arp2/3 complex (actin-related protein 2/3 complex)-dependent actin polymerization. In the early 1990s, the development of powerful genetic tools in protozoa and mammals and discovery of these motors in yeast allowed the demonstration of their roles in membrane traffic along the endocytic and secretory pathways, in vacuole contraction, in cell motility and in mechanosensing. The powerful yeast genetics has contributed towards dissecting in detail the function and regulation of Saccharomyces cerevisiae myosins-I Myo3 and Myo5 in endocytic budding from the plasma membrane. In the present review, we summarize the evidence, dissecting their exact role in membrane budding and the molecular mechanisms controlling their recruitment and biochemical activities at the endocytic sites.

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“…WIP suppresses growth defects of the S. cerevisiae end5/vrp1 mutant (Vaduva et al, 1999). ScEnd5/Vrp1 is a very proline-rich protein that is involved in cytoskeletal organization and can interact with both Las17 and Myo5 (Anderson et al, 1998;Evangelista et al, 2000;Munn & Thanabalu, 2009). The temperature sensitivity and loss of viability of an end5-1/vrp1 mutant can be suppressed by the overexpression of ScLAS17 (Naqvi et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Candida albicans Vrp1 is required for polarized morphogenesis and interacts with Wal1 and Myo5

et al. 2010

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Recently, a link between endocytosis and hyphal morphogenesis has been identified in Candida albicans via the Wiskott-Aldrich syndrome gene homologue WAL1. To get a more detailed mechanistic understanding of this link we have investigated a potentially conserved interaction between Wal1 and the C. albicans WASP-interacting protein (WIP) homologue encoded by VRP1. Deletion of both alleles of VRP1 results in strong hyphal growth defects under serum inducing conditions but filamentation can be observed on Spider medium. Mutant vrp1 cells show a delay in endocytosis -measured as the uptake and delivery of the lipophilic dye FM4-64 into small endocytic vesicles -compared to the wild-type. Vacuolar morphology was found to be fragmented in a subset of cells and the cortical actin cytoskeleton was depolarized in vrp1 daughter cells. The morphology of the vrp1 null mutant could be complemented by reintegration of the wild-type VRP1 gene at the BUD3 locus. Using the yeast two-hybrid system we could demonstrate an interaction between the C-terminal part of Vrp1 and the N-terminal part of Wal1, which contains the WH1 domain. Furthermore, we found that Myo5 has several potential interaction sites on Vrp1. This suggests that a Wal1-Vrp1-Myo5 complex plays an important role in endocytosis and the polarized localization of the cortical actin cytoskeleton to promote polarized hyphal growth in C. albicans.

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Verprolin: A cool set of actin‐binding sites and some very HOT prolines

Cited by 9 publications

References 32 publications

Actin Dosage Lethality Screening in Yeast Mediated by Selective Ploidy Ablation Reveals Links to Urmylation/Wobble Codon Recognition and Chromosome Stability

Actin Dosage Lethality Screening in Yeast Mediated by Selective Ploidy Ablation Reveals Links to Urmylation/Wobble Codon Recognition and Chromosome Stability

Function and regulation of Saccharomyces cerevisiae myosins-I in endocytic budding

Candida albicans Vrp1 is required for polarized morphogenesis and interacts with Wal1 and Myo5

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