Kif5b controls the localization of myofibril components for their assembly and linkage to the myotendinous junctions

Author:

Wang Zai12,Cui Ju13,Wong Wai Man4,Li Xiuling1,Xue Wenqian1,Lin Raozhou1,Wang Jing1,Wang Peigang5,Tanner Julian A.1,Cheah Kathryn S. E.1,Wu Wutian4,Huang Jian-Dong1

Affiliation:

1. Department of Biochemistry, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong

2. Institute of Clinical Medical Sciences, China-Japan Friendship Hospital, Beijing, China

3. Beijing Institute of Geriatrics, Beijing Hospital, Ministry of Health, Beijing, China

4. Department of Anatomy, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong

5. HKU-Pasteur Research Centre, The University of Hong Kong, Hong Kong

Abstract

Controlled delivery of myofibril components to the appropriate sites of assembly is crucial for myofibrillogenesis. Here, we show that kinesin-1 heavy chain Kif5b plays important roles in anterograde transport of α-sarcomeric actin, non-muscle myosin IIB, together with intermediate filament proteins desmin and nestin to the growing tips of the elongating myotubes. Mice with Kif5b conditionally knocked out in myogenic cells showed aggregation of actin filaments and intermediate filament proteins in the differentiating skeletal muscle cells, which further affected myofibril assembly and their linkage to the myotendinous junctions. The expression of Kif5b in mutant myotubes rescued the localization of the affected proteins. Functional mapping of Kif5b revealed a 64-amino acid α-helix domain in the tail region, which directly interacted with desmin and might be responsible for the transportation of these proteins in a complex.

Publisher

The Company of Biologists

Subject

Developmental Biology,Molecular Biology

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