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Article Dans Une Revue Journal of Biomedicine and Biotechnology Année : 2011

Tissue expression and actin binding of a novel N-terminal utrophin isoform.

Résumé

Utrophin and dystrophin present two large proteins that link the intracellular actin cytoskeleton to the extracellular matrix via the C-terminal-associated protein complex. Here we describe a novel short N-terminal isoform of utrophin and its protein product in various rat tissues (N-utro, 62 kDa, amino acids 1-539, comprising the actin-binding domain plus the first two spectrin repeats). Using different N-terminal recombinant utrophin fragments, we show that actin binding exhibits pronounced negative cooperativity (affinity constants K(1) = -5 × 10(6) and K(2) =-1 × 10(5 )M(-1)) and is Ca(2+)-insensitive. Expression of the different fragments in COS7 cells and in myotubes indicates that the actin-binding domain alone binds exclusively to actin filaments. The recombinant N-utro analogue binds in vitro to actin and in the cells associates to the membranes. The results indicate that N-utro may be responsible for the anchoring of the cortical actin cytoskeleton to the membranes in muscle and other tissues.

Dates et versions

hal-02880220 , version 1 (24-06-2020)

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Citer

Richard Zuellig, Beat Bornhauser, Ralf Amstutz, Bruno Constantin, Marcus Schaub. Tissue expression and actin binding of a novel N-terminal utrophin isoform.. Journal of Biomedicine and Biotechnology, 2011, 2011, pp.904547. ⟨10.1155/2011/904547⟩. ⟨hal-02880220⟩

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