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First published online 14 November 2006
doi: 10.1242/jcs.03255
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Research Article |
1 Clinic of Dermatology, University Hospital, Geneva, Rue Micheli-du-Crest 14, 1211-Geneva 14, Switzerland
2 Division of Endocrinology, Diabetology and Nutrition, University Hospital, Geneva, Rue Micheli-du-Crest 14, 1211-Geneva 14, Switzerland
3 Biologie Moléculaire de la Différenciation, Université Paris-7, 2 Place Jussieu, 75005 Paris, France
4 Departments of Pathology and Dermatology, Feinberg School of Medicine, Northwestern University, 303 E. Chicago Avenue, Chicago, IL 60611, USA
¶ Author for correspondence (e-mail: luca.borradori{at}hcuge.ch)
Accepted 11 September 2006
Desmosomes are intercellular adhesive complexes that anchor the intermediate filament cytoskeleton to the cell membrane in epithelia and cardiac muscle cells. The desmosomal component desmoplakin plays a key role in tethering various intermediate filament networks through its C-terminal plakin repeat domain. To gain better insight into the cytoskeletal organization of cardiomyocytes, we investigated the association of desmoplakin with desmin by cell transfection, yeast two-hybrid, and/or in vitro binding assays. The results indicate that the association of desmoplakin with desmin depends on sequences within the linker region and C-terminal extremity of desmoplakin, where the B and C subdomains contribute to efficient binding; a potentially phosphorylatable serine residue in the C-terminal extremity of desmoplakin affects its association with desmin; the interaction of desmoplakin with non-filamentous desmin requires sequences contained within the desmin C-terminal rod portion and tail domain in yeast, whereas in in vitro binding studies the desmin tail is dispensable for association; and mutations in either the C-terminus of desmoplakin or the desmin tail linked to inherited cardiomyopathy seem to impair desmoplakindesmin interaction. These studies increase our understanding of desmoplakin-intermediate filament interactions, which are important for maintenance of cytoarchitecture in cardiomyocytes, and give new insights into the molecular basis of desmoplakin- and desmin-related human diseases.
Key words: Desmoplakin, Desmin, Vimentin, Intermediate filaments, Cardiomyocyte, Cardiomyopathy
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