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Biochem Soc Trans

Title:		"Interactions between Sla1p, Lsb5p and Arf3p in yeast endocytosis"
Author(s):		Costa R; Ayscough KR;
Address:		"Department of Molecular Biology and Biotechnology, Firth Court, University of Sheffield, Western Bank, Sheffield S10 2TN, UK"
Journal Title:		Biochem Soc Trans
Year:		2005
Volume:		33
Issue:		Pt 6
Page Number:		1273 - 1275
DOI:		10.1042/BST0331273
ISSN/ISBN:		0300-5127 (Print) 0300-5127 (Linking)
Abstract:		"Endocytosis is critical for controlling the protein-lipid composition of the plasma membrane, uptake of nutrients as well as pathogens, and also plays an important role in regulation of cell signalling. While a number of pathways for endocytosis have been characterized in different organisms, all of these require remodelling of the cell cortex. The importance of a dynamic actin cytoskeleton for facilitating endocytosis has been recognized for many years in budding yeast, and is increasingly supported by studies in mammalian cells. Our studies have focused on proteins that we have shown to act at the interface between the actin cytoskeleton and the endocytic machinery. In particular, we have studied interactions of Sla1p, which binds to both activators of actin dynamics, i.e. Abp1p, Las17p and Pan1p, and to cargo proteins such as the pheromone receptor Ste2p. More recently we have mapped the interaction of Sla1p with Lsb5p, a protein that has a similar structure to the GGA [Golgi-localizing, gamma-adaptin ear homology domain, Arf (ADP-ribosylation factor)-binding] family of proteins with an N-terminal VHS (Vps27p/Hrs/STAM)-domain and a GAT (GGAs and TOM1) domain. We show that Lsb5p can interact with yeast Arf3p (orthologous with mammalian Arf6) and we demonstrate a requirement for Arf3p expression in order to localize Lsb5p to the cell cortex"
Keywords:		ADP-Ribosylation Factors/*metabolism Actins/metabolism Animals Carrier Proteins/*metabolism Cell Membrane/metabolism Cytoskeletal Proteins Cytoskeleton/metabolism Endocytosis/*physiology Microfilament Proteins/*metabolism Saccharomyces cerevisiae/cytology;
Notes:		"MedlineCosta, R Ayscough, K R eng Research Support, Non-U.S. Gov't England 2005/10/26 Biochem Soc Trans. 2005 Dec; 33(Pt 6):1273-5. doi: 10.1042/BST0331273"