Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 456K) PPT slides of all figures Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Correia, I. Articles by Matsudaira, P. Search for Related Content PubMed PubMed Citation Articles by Correia, I. Articles by Matsudaira, P. Pubmed/NCBI databases Substance via MeSH Related Collections Related Article Social Bookmarking                            What's this?

© The Rockefeller University Press, 0021-9525/1999//831 $5.00
The Journal of Cell Biology, Volume 146, Number 4, , 1999 831-842

Integrating the Actin and Vimentin Cytoskeletons

Ivan Correia^a, Donald Chu^a, Ying-Hao Chou^c, Robert D. Goldman^c, and Paul Matsudaira^a,b

^a Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02142
^b Department of Biology and Division of Bioengineering and Environmental Health, Massachusetts Institute of Technology, Cambridge, Massachusetts 02142
^c Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60208
Whitehead Institute of Biomedical Research, 9 Cambridge Center, Cambridge, MA 02142.(617) 258-6691(617) 258-5206

correia{at}wi.mit.edu

Cells adhere to the substratum through specialized structures that are linked to the actin cytoskeleton. Recent studies report that adhesion also involves the intermediate filament (IF) and microtubule cytoskeletons, although their mechanisms of interaction are unknown. Here we report evidence for a novel adhesion-dependent interaction between components of the actin and IF cytoskeletons. In biochemical fractionation experiments, fimbrin and vimentin coprecipitate from detergent extracts of macrophages using vimentin- or fimbrin-specific antisera. Fluorescence microscopy confirms the biochemical association. Both proteins colocalized to podosomes in the earliest stages of cell adhesion and spreading. The complex is also found in filopodia and retraction fibers. After detergent extraction, fimbrin and vimentin staining of podosomes, filopodia, and retraction fibers are lost, confirming that the complex is localized to these structures. A 1:4 stoichiometry of fimbrin binding to vimentin and a low percentage (1%) of the extracted vimentin suggest that fimbrin interacts with a vimentin subunit. A fimbrin-binding site was identified in the NH₂-terminal domain of vimentin and the vimentin binding site at residues 143–188 in the CH1 domain of fimbrin. Based on these observations, we propose that a fimbrin–vimentin complex may be involved in directing the assembly of the vimentin cytoskeleton at cell adhesion sites.

Key Words: fimbrin • vimentin • cytoskeleton • adhesion • microfilaments

© 1999 The Rockefeller University Press

CiteULike

Complore

Connotea

Del.icio.us

Digg

Facebook

Reddit

Technorati

Twitter

This article has been cited by other articles:

• Chou, Y.-H., Goldman, R. D. (2000). Intermediate Filaments on the Move. JCB 150: 101-106 [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents