Novel proteins linking the actin cytoskeleton to the endocytic machinery in Saccharomyces cerevisiae

Dewar, H. and Warren, D.T. and Gardiner, F.C. and Gourlay, Campbell W. and Satish, N. and Richardson, M.R. and Andrews, P.D. and Ayscough, K.R. (2002) Novel proteins linking the actin cytoskeleton to the endocytic machinery in Saccharomyces cerevisiae. Molecular Biology of the Cell, 13 (10). pp. 3646-3661. ISSN 1059-1524 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1091/mbc.E02-05-0262

Abstract

The importance of coupling the process of endocytosis to factors regulating actin dynamics has been clearly demonstrated in yeast, and many proteins involved in these mechanisms have been identified and characterized. Here we demonstrate the importance of two additional cortical components, Ysc84p and Lsb5p, which together are essential for the organization of the actin cytoskeleton and for fluid phase endocytosis. Both Ysc84p and Lsb5p were identified through two-hybrid screens with different domains of the adaptor protein Sla1p. Ysc84p colocalizes with cortical actin and requires the presence of an intact actin cytoskeleton for its cortical localization. Ycl034w/Lsb5p localizes to the cell cortex but does not colocalize with actin. The Lsb5 protein contains putative VHS and GAT domains as well as an NPF motif, which are all domains characteristic of proteins involved in membrane trafficking. Deletion of either gene alone does not confer any dramatic phenotype on cells. However, deletion of both genes is lethal at elevated temperatures. Furthermore, at all temperatures this double mutant has depolarized actin and an almost undetectable level of fluid phase endocytosis. Our data demonstrate that Ysc84p and Lsb5p are important components of complexes involved in overlapping pathways coupling endocytosis with the actin cytoskeleton in yeast.

Item Type: Article
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Campbell Gourlay
Date Deposited: 30 Sep 2009 15:18
Last Modified: 09 Aug 2013 08:07
Resource URI: http://kar.kent.ac.uk/id/eprint/22650 (The current URI for this page, for reference purposes)
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