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- The unique insert in myosin VI is a structural calcium–calmodulin binding site
The unique insert in myosin VI is a structural calcium–calmodulin binding site
Auteurs
Amel Bahloul, Guillaume Chevreux, Amber L. Wells, Davy Martin, Jocelyn Nolt, Zhaohui Yang, Li-Qiong Chen, Noëlle Potier, Alain Van Dorsselaer, Steve Rosenfeld, Anne Houdusse, H. Lee Sweeney
Résumé
Myosin VI contains an inserted sequence that is unique among myosin superfamily members and has been suggested to be a determinant of the reverse directionality and unusual motility of the motor. It is thought that each head of a two-headed myosin VI molecule binds one calmodulin (CaM) by means of a single “IQ motif”. Using truncations of the myosin VI protein and electrospray ionization(ESI)-MS, we demonstrate that in fact each myosin VI head binds two CaMs. One CaM binds to a conventional IQ motif either with or without calcium and likely plays a regulatory role when calcium binds to its N-terminal lobe. The second CaM binds to a unique insertion between the converter region and IQ motif. This unusual CaM-binding site normally binds CaM with four Ca
Membres
