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J. Biol. Chem., Vol. 278, Issue 8, 5864-5870, February 21, 2003
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From the V-1 is a 12-kDa protein consisting of three
consecutive ANK repeats, which are believed to serve as the surface for
protein-protein interactions. It is thought to have a role in neural
development for its temporal profile of expression during murine
cerebellar development, but its precise role remains unknown. Here we
applied the proteomic approach to search for protein targets that
interact with V-1. The V-1 cDNA attached with a tandem affinity
purification tag was expressed in the cultured 293T cells, and the
protein complex formed within the cells were captured and characterized by mass spectrometry. We detected two polypeptides specifically associated with V-1, which were identified as the
V-1, a Protein Expressed Transiently during Murine Cerebellar
Development, Regulates Actin Polymerization via Interaction with
Capping Protein*
§,,,,
, and¶**
Department of Chemistry, Graduate School of
Science, Tokyo Metropolitan University, Hachioji-shi, Tokyo 192-0397, Japan, ¶ Integrated Proteomics System Project, Pioneer Research on
Genome the Frontier, Ministry of Education, Culture, Sports, Science
and Technology, Department of Chemistry, Graduate School of Science,
Tokyo Metropolitan University, Hachioji-shi, Tokyo 192-0397, Japan,
Department of Biology, Faculty of Science, Chiba University,
Chiba 263-8522, Japan, and ** Division of Proteomics
Research (ABJ-Millipore), The Institute of Medical Science, The
University of Tokyo, Minato-ku, Tokyo 108-8639, Japan
and 
subunits of the capping protein (CP, alternatively called CapZ or
-actinin). CP regulates actin polymerization by capping the
barbed end of the actin filament. The V-1·CP complex was
detected not only in cultured cells transfected with the V-1 cDNA
but also endogenously in cells as well as in murine cerebellar
extracts. An analysis of the V-1/CP interaction by surface
plasmon resonance spectroscopy showed that V-1 formed a stable complex
with the CP heterodimer with a dissociation constant of 1.2 × 10
7 M and a molecular stoichiometry of
~1:1. In addition, V-1 inhibited the CP-regulated actin
polymerization in vitro in a dose-dependent manner. Thus, our results suggest that V-1 is a novel component that
regulates the dynamics of actin polymerization by interacting with CP
and thereby participates in a variety of cellular processes such as
actin-driven cell movements and motility during neuronal development.
*
This study was supported in part by grants for the
Integrated Proteomics System Project and Pioneer Research on Genome the Frontier from the Ministry of Education, Culture, Sports, Science and
Technology of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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