Background: Plectin, a member of the plakin family proteins, is a high molecular weight protein that is ubiquitously expressed. It acts as a cytolinker for the three major components of the cyotoskeleton, namely actin microfilaments, microtubules and intermediate filaments.
Objective: The aim of our experiments was to identify new binding sites for intermediate filaments on plectin and to specify these sites.
Methods: We introduced truncated forms of plectin into several cell lines and observe interaction between plectin and intermediate filaments.
Results: We found that a linker region in the COOH-terminal end of plectin was required for the association of the protein with intermediate filaments. In addition, we also demonstrated that a serine residue at position 4645 of plectin may have a role on binding of plectin to intermediate filaments.
Conclusion: A linker region in the COOH-terminal end and serine residue at position 4645 may be important for the binding of plectin to intermediate filaments.
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