Verprolin function in endocytosis and actin organization - Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain

Thanabalu, T., Rajmohan, R., Meng, L., Ren, G., Vajjhala, P. R. and Munn, A. L. (2007) Verprolin function in endocytosis and actin organization - Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain. FEBS Journal, 274 16: 4103-4125. doi:10.1111/j.1742-4658.2007.05936.x


Author Thanabalu, T.
Rajmohan, R.
Meng, L.
Ren, G.
Vajjhala, P. R.
Munn, A. L.
Title Verprolin function in endocytosis and actin organization - Roles of the Las17p (yeast WASP)-binding domain and a novel C-terminal actin-binding domain
Journal name FEBS Journal   Check publisher's open access policy
ISSN 1742-464X
1742-4658
Publication date 2007
Sub-type Article (original research)
DOI 10.1111/j.1742-4658.2007.05936.x
Volume 274
Issue 16
Start page 4103
End page 4125
Total pages 23
Place of publication United Kingdom
Publisher Wiley-Blackwell
Collection year 2008
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
730102 Immune system and allergy
Abstract Vrp1p (verprolin.. End5p) is the yeast ortholog of human Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP). Vrp1p localizes to the cortical actin cytoskeleton, is necessary for its polarization to sites of growth and is also essential for endocytosis. At elevated temperature, Vrp1p becomes essential for growth. A C-terminal Vrplp fragment (C-Vrp1p) retains the ability to localize to the cortical actin cytoskeleton and function in actin-cytoskeleton polarization, endocytosis and growth. Here, we demonstrate that two submodules in C-Vrp1p are required for actin-cytoskeleton polarization: a novel C-terminal actin-binding submodule (CABS) that contains a novel G-actin-binding domain, which we call a verprolin homology 2 C-terminal (VH2-C) domain; and a second submodule comprising the Las17p-binding domain (LBD) that binds Las17p (yeast WASP). The LBD localizes C-Vrp1p to membranes and the cortical actin cytoskeleton. Intriguingly, the LBD is sufficient to restore endocytosis and growth at elevated temperature to Vrplp-deficient cells. The CABS also restores these functions, but only if modified by a lipid anchor to provide membrane association. Our findings highlight the role of Las17p binding for Vrplp membrane association, suggest general membrane association may be more important than specific targeting to the cortical actin cytoskeleton for Vrplp function in enclocytosis and cell growth, and suggest that Vrplp binding to individual effectors may alter their physiological activity.
Keyword Biochemistry & Molecular Biology
actin patch
Arp2/3
Bee1p
cell polarity
WH2 domain
Wiskott-aldrich-syndrome
Wasp-interacting Protein
Yeast Myosin-i
Saccharomyces-cerevisiae
Arp2/3 Complex
N-wasp
Mediated Endocytosis
Family Protein
Budding Yeast
Cell-cycle
Q-Index Code C1
Q-Index Status Confirmed Code

 
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Created: Mon, 18 Feb 2008, 14:51:08 EST