Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.01239
Title: The yeast dynamin-related GTPase Vps1p functions in the organization of the actin cytoskeleton via interaction with Sla1p
Authors: Yu, X.
Cai, M. 
Keywords: Actin
Dynamin
GTPase
Sla1p
Vps1p
Issue Date: 1-Aug-2004
Source: Yu, X., Cai, M. (2004-08-01). The yeast dynamin-related GTPase Vps1p functions in the organization of the actin cytoskeleton via interaction with Sla1p. Journal of Cell Science 117 (17) : 3839-3853. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.01239
Abstract: Recent studies have suggested that the function of the large GTPase dynamin in endocytosis in mammalian cells may comprise a modulation of actin cytoskeleton. The role of dynamin in actin cytoskeleton organization in the yeast Saccharomyces cerevisiae has remained undefined. In this report, we found that one of the yeast dynamin-related proteins, Vps1p, is required for normal actin cytoskeleton organization. At both permissive and non-permissive temperatures, the vps1 mutants exhibited various degrees of phenotypes commonly associated with actin cytoskeleton defects: depolarized and aggregated actin structures, hypersensitivity to the actin cytoskeleton toxin latrunculin-A, randomized bud site selection and chitin deposition, and impaired efficiency in the internalization of membrane receptors. Over-expression of the GTPase mutants of vps1 also led to actin abnormalities. Consistent with these actin-related defects, Vps1p was found to interact physically, and partially co-localize, with the actin-regulatory protein Sla1p. The normal cellular localization of Sla1p required Vps1p and could be altered by over-expression of a region of Vps1p that was involved in the interaction with Sla1p. The same region also promoted mis-sorting of the vacuolar protein carboxypeptidase Y upon over-expression. These findings suggest that the functions of the dynamin-related protein Vps1p in actin cytoskeleton dynamics and vacuolar protein sorting are probably related to each other.
Source Title: Journal of Cell Science
URI: http://scholarbank.nus.edu.sg/handle/10635/113689
ISSN: 00219533
DOI: 10.1242/jcs.01239
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