Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Verprolin: A cool set of actin‐binding sites and some very HOT prolines

Verprolin: A cool set of actin‐binding sites and some very HOT prolines Spatiotemporal organisation of eukaryotic cells is established and maintained by the cytoskeleton, a highly dynamic and complex network of structural and signalling proteins. Many components of the cytoskeleton are functionally and structurally conserved between humans and yeast. Among these are verprolin (Vrp1p) in yeast and its human ortholog Wiskott‐Aldrich syndrome protein (WASP)‐interacting protein (WIP). Much of our understanding of the function of these proteins has come from genetic analysis in yeast. Verprolin‐deficient yeast cells exhibit defects in cytokinesis, endocytosis, and actin cytoskeleton polarisation. Verprolin binds actin, the yeast ortholog of human WASP (Las17p or Bee1p), and the yeast ortholog of human PSTPIP1 (Hof1p or Cyk2p). We propose that verprolin acts as a chaperone that by transient bimolecular interactions maintains the proper function of its partners. Verprolin‐related proteins and partners are implicated in cancer, immunodeficiency, and neurodegeneration. Therefore, elucidating how verprolin functions will have major impacts in cell biology and medicine. © 2009 IUBMB IUBMB Life 61(7): 707–712, 2009 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png IUBMB Life Wiley

Verprolin: A cool set of actin‐binding sites and some very HOT prolines

IUBMB Life , Volume 61 (7) – Jul 1, 2009

Loading next page...
 
/lp/wiley/verprolin-a-cool-set-of-actin-binding-sites-and-some-very-hot-prolines-kpurJ0LmRs

References (31)

Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Copyright © 2009 International Union of Biochemistry and Molecular Biology, Inc.
ISSN
1521-6543
eISSN
1521-6551
DOI
10.1002/iub.195
pmid
19507265
Publisher site
See Article on Publisher Site

Abstract

Spatiotemporal organisation of eukaryotic cells is established and maintained by the cytoskeleton, a highly dynamic and complex network of structural and signalling proteins. Many components of the cytoskeleton are functionally and structurally conserved between humans and yeast. Among these are verprolin (Vrp1p) in yeast and its human ortholog Wiskott‐Aldrich syndrome protein (WASP)‐interacting protein (WIP). Much of our understanding of the function of these proteins has come from genetic analysis in yeast. Verprolin‐deficient yeast cells exhibit defects in cytokinesis, endocytosis, and actin cytoskeleton polarisation. Verprolin binds actin, the yeast ortholog of human WASP (Las17p or Bee1p), and the yeast ortholog of human PSTPIP1 (Hof1p or Cyk2p). We propose that verprolin acts as a chaperone that by transient bimolecular interactions maintains the proper function of its partners. Verprolin‐related proteins and partners are implicated in cancer, immunodeficiency, and neurodegeneration. Therefore, elucidating how verprolin functions will have major impacts in cell biology and medicine. © 2009 IUBMB IUBMB Life 61(7): 707–712, 2009

Journal

IUBMB LifeWiley

Published: Jul 1, 2009

Keywords: actin; cell division; cell polarity; membrane traffic

There are no references for this article.