Document Detail


Arabidopsis VILLIN1 and VILLIN3 have overlapping and distinct activities in actin bundle formation and turnover.
MedLine Citation:
PMID:  20807878     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Actin filament bundles are higher-order cytoskeletal structures that are crucial for the maintenance of cellular architecture and cell expansion. They are generated from individual actin filaments by the actions of bundling proteins like fimbrins, LIMs, and villins. However, the molecular mechanisms of dynamic bundle formation and turnover are largely unknown. Villins belong to the villin/gelsolin/fragmin superfamily and comprise at least five isovariants in Arabidopsis thaliana. Different combinations of villin isovariants are coexpressed in various tissues and cells. It is not clear whether these isovariants function together and act redundantly or whether they have unique activities. VILLIN1 (VLN1) is a simple filament-bundling protein and is Ca(2+) insensitive. Based on phylogenetic analyses and conservation of Ca(2+) binding sites, we predict that VLN3 is a Ca(2+)-regulated villin capable of severing actin filaments and contributing to bundle turnover. The bundling activity of both isovariants was observed directly with time-lapse imaging and total internal reflection fluorescence (TIRF) microscopy in vitro, and the mechanism mimics the "catch and zipper" action observed in vivo. Using time-lapse TIRF microscopy, we observed and quantified the severing of individual actin filaments by VLN3 at physiological calcium concentrations. Moreover, VLN3 can sever actin filament bundles in the presence of VLN1 when calcium is elevated to micromolar levels. Collectively, these results demonstrate that two villin isovariants have overlapping and distinct activities.
Authors:
Parul Khurana; Jessica L Henty; Shanjin Huang; Andrew M Staiger; Laurent Blanchoin; Christopher J Staiger
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2010-08-31
Journal Detail:
Title:  The Plant cell     Volume:  22     ISSN:  1532-298X     ISO Abbreviation:  Plant Cell     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-09-29     Completed Date:  2011-01-13     Revised Date:  2011-08-03    
Medline Journal Info:
Nlm Unique ID:  9208688     Medline TA:  Plant Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2727-48     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-2064, USA.
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MeSH Terms
Descriptor/Qualifier:
Actins / biosynthesis*
Arabidopsis / genetics*,  metabolism
Arabidopsis Proteins / genetics,  metabolism*
Binding Sites
Calcium / metabolism
Microfilament Proteins / genetics,  metabolism*
Protein Isoforms / genetics,  metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Arabidopsis Proteins; 0/Microfilament Proteins; 0/Protein Isoforms; 0/villin; 7440-70-2/Calcium
Comments/Corrections

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