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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Huang, Shanjin Robinson, Robert C. Gao, Lisa Y. Matsumoto, Tracie Brunet, Arnaud Blanchoin, Laurent Staiger, Christopher J. |
| Description | Country affiliation: United States Author Affiliation: Huang S ( Department of Biological Sciences and Purdue Motility Group, Purdue University, West Lafayette, Indiana 47907-2064, USA.) |
| Abstract | Dynamic cytoplasmic streaming, organelle positioning, and nuclear migration use molecular tracks generated from actin filaments arrayed into higher-order structures like actin cables and bundles. How these arrays are formed and stabilized against cellular depolymerizing forces remains an open question. Villin and fimbrin are the best characterized actin-filament bundling or cross-linking proteins in plants and each is encoded by a multigene family of five members in Arabidopsis thaliana. The related villins and gelsolins are conserved proteins that are constructed from a core of six homologous gelsolin domains. Gelsolin is a calcium-regulated actin filament severing, nucleating and barbed end capping factor. Villin has a seventh domain at its C terminus, the villin headpiece, which can bind to an actin filament, conferring the ability to crosslink or bundle actin filaments. Many, but not all, villins retain the ability to sever, nucleate, and cap filaments. Here we have identified a putative calcium-insensitive villin isoform through comparison of sequence alignments between human gelsolin and plant villins with x-ray crystallography data for vertebrate gelsolin. VILLIN1 (VLN1) has the least well-conserved type 1 and type 2 calcium binding sites among the Arabidopsis VILLIN isoforms. Recombinant VLN1 binds to actin filaments with high affinity (K(d) approximately 1 microM) and generates bundled filament networks; both properties are independent of the free Ca(2+) concentration. Unlike human plasma gelsolin, VLN1 does not nucleate the assembly of filaments from monomer, does not block the polymerization of profilin-actin onto barbed ends, and does not stimulate depolymerization or sever preexisting filaments. In kinetic assays with ADF/cofilin, villin appears to bind first to growing filaments and protects filaments against ADF-mediated depolymerization. We propose that VLN1 is a major regulator of the formation and stability of actin filament bundles in plant cells and that it functions to maintain the cable network even in the presence of stimuli that result in depolymerization of other actin arrays. |
| File Format | HTM / HTML |
| ISSN | 10404651 |
| e-ISSN | 1531298X |
| Journal | THE PLANT CELL ONLINE |
| Issue Number | 2 |
| Volume Number | 17 |
| Language | English |
| Publisher | American Society of Plant Biologists |
| Publisher Date | 2005-02-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Botany Actin Cytoskeleton Metabolism Actins Arabidopsis Proteins Amino Acid Sequence Arabidopsis Genetics Binding Sites Calcium Calcium-binding Proteins Kinetics Molecular Sequence Data Molecular Weight Protein Binding Recombinant Proteins Sequence Homology, Amino Acid Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Plant Science |
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