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Journal of Cell Science 114, 2065-2076 (2001)
© 2001 The Company of Biologists Limited

RESEARCH ARTICLE

The interaction of plectin with actin: evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin

Lionel Fontao*,§, Dirk Geerts{ddagger},§, Ingrid Kuikman, Jan Koster, Duco Kramer and Arnoud Sonnenberg

The Netherlands Cancer Institute, Division of Cell Biology, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
* Present address: Department of Dermatology, Geneva University Hospital, 24 rue Micheli-Ducrest, 1211 Geneva 4, Switzerland
{ddagger} Present address: Department of Human Genetics M1-159, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands
§ L. Fontao and D. Geerts contributed equally to this work

¶Author for correspondence (e-mail: asonn{at}nki.nl)

Accepted March 9, 2001

Plectin is a major component of the cytoskeleton and is expressed in a wide variety of cell types. It plays an important role in the integrity of the cytoskeleton by cross-linking the three filamentous networks and stabilizing cell-matrix and cell-cell contacts. Sequence analysis showed that plectin contains a highly conserved actin-binding domain, consisting of a pair of calponin-like subdomains. Using yeast two-hybrid assays in combination with in vitro binding experiments, we demonstrate that the actin-binding domain of plectin is fully functional and preferentially binds to polymeric actin. The sequences required for actin binding were identified at the C-terminal end of the first calponin homology domain within the actin-binding domain of plectin. We found that the actin-binding domain of plectin is able to bundle actin filaments and we present evidence that this is mediated by the dimerization of this domain. In addition we also show that plectin and another member of the plakin family, dystonin, can heterodimerize by their actin-binding domains. We propose a new mechanism by which plectin and possibly also other actin-binding proteins can regulate the organization of the F-actin network in the cell.

Key words: Plectin, Dystrophin, Actin-binding domain, Focal contact




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© The Company of Biologists Ltd 2001