A proline‐rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae
- 1 November 1993
- journal article
- research article
- Published by Wiley in Molecular Microbiology
- Vol. 10 (3) , 585-596
- https://doi.org/10.1111/j.1365-2958.1993.tb00930.x
Abstract
A gene (VRP1) encoding a novel proline-rich protein (verprolin) has been isolated from the yeast Saccharomyces cerevisiae as a result of its hybridization to a chick vinculin cDNA probe. The deduced protein sequence contains 24% proline residues present as proline-rich motifs throughout the verprolin sequence. Several of these motifs resemble recently identified sequences shown to bind Src homology 3 (SH3) domains in vitro. Replacement of the wild-type VRP1 allele with a mutant allele results in strains that grow slower than wild-type strains and are temperature sensitive. The vrp1 mutants are impaired in both cell shape and size and display aberrant chitin and actin localization. We propose that verporlin is involved in the maintenance of the yeast actin cytoskeleton, through interactions with other proteins, possibly containing SH3 domains.Keywords
This publication has 63 references indexed in Scilit:
- Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex.The Journal of cell biology, 1993
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993
- The small GTP-binding protein rac regulates growth factor-induced membrane rufflingCell, 1992
- The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factorsCell, 1992
- Phospholipase C-β1 is a GTPase-activating protein for Gq/11, its physiologic regulatorCell, 1992
- SH3 — an abundant protein domain in search of a functionFEBS Letters, 1992
- The yeast type II myosin heavy chain: Analysis of its predicted polypeptide sequenceJournal of Muscle Research and Cell Motility, 1991
- Microfilament-membrane interactionTrends in Biochemical Sciences, 1985
- Electron microscopy of rotary shadowed vinculin and vinculin complexesJournal of Molecular Biology, 1985
- Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces.The Journal of cell biology, 1984