Favre, Bertrand; Schneider, Yann; Lingasamy, Prakash; Bouameur, Jamal-Eddine; Begré, Nadja; Gontier, Yves; Steiner-Champliaud, Marie-France; Frias, Miguel A; Borradori, Luca; Fontao, Lionel (2011). Plectin interacts with the rod domain of type III intermediate filament proteins desmin and vimentin. European journal of cell biology, 90(5), pp. 390-400. Jena: Urban & Fischer 10.1016/j.ejcb.2010.11.013
Full text not available from this repository.Plectin is a versatile cytolinker protein critically involved in the organization of the cytoskeletal filamentous system. The muscle-specific intermediate filament (IF) protein desmin, which progressively replaces vimentin during differentiation of myoblasts, is one of the important binding partners of plectin in mature muscle. Defects of either plectin or desmin cause muscular dystrophies. By cell transfection studies, yeast two-hybrid, overlay and pull-down assays for binding analysis, we have characterized the functionally important sequences for the interaction of plectin with desmin and vimentin. The association of plectin with both desmin and vimentin predominantly depended on its fifth plakin repeat domain and downstream linker region. Conversely, the interaction of desmin and vimentin with plectin required sequences contained within the segments 1A-2A of their central coiled-coil rod domain. This study furthers our knowledge of the interaction between plectin and IF proteins important for maintenance of cytoarchitecture in skeletal muscle. Moreover, binding of plectin to the conserved rod domain of IF proteins could well explain its broad interaction with most types of IFs.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Department of Dermatology, Urology, Rheumatology, Nephrology, Osteoporosis (DURN) > Clinic of Dermatology |
UniBE Contributor: |
Favre, Bertrand, Lingasamy, Prakash, Borradori, Luca |
ISSN: |
0171-9335 |
Publisher: |
Urban & Fischer |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 14:21 |
Last Modified: |
05 Dec 2022 14:06 |
Publisher DOI: |
10.1016/j.ejcb.2010.11.013 |
PubMed ID: |
21296452 |
Web of Science ID: |
000289967600003 |
URI: |
https://boris.unibe.ch/id/eprint/7059 (FactScience: 212208) |
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