期刊
EUROPEAN JOURNAL OF CELL BIOLOGY
卷 90, 期 5, 页码 390-400出版社
ELSEVIER GMBH
DOI: 10.1016/j.ejcb.2010.11.013
关键词
Plectin; Plakin; Desmin; Vimentin; Intermediate filaments
类别
资金
- Swiss National Foundation for Research [3100A0-121966]
- Swiss Foundation for Research on Muscle Diseases
- Association Francaise contre les Myopathies (Paris)
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. (C) 2010 Elsevier GmbH. All rights reserved.
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