pubmed.ncbi.nlm.nih.gov

Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling - PubMed

doi: 10.1038/nsmb.2923. Epub 2014 Dec 1.

Affiliations

Structure of myosin-1c tail bound to calmodulin provides insights into calcium-mediated conformational coupling

Qing Lu et al. Nat Struct Mol Biol. 2015 Jan.

Abstract

Class I myosins can sense cellular mechanical forces and function as tension-sensitive anchors or transporters. How mechanical load is transduced from the membrane-binding tail to the force-generating head in myosin-1 is unknown. Here we determined the crystal structure of the entire tail of mouse myosin-1c in complex with apocalmodulin, showing that myosin-1c adopts a stable monomer conformation suited for force transduction. The lever-arm helix and the C-terminal extended PH domain of the motor are coupled by a stable post-IQ domain bound to calmodulin in a highly unusual mode. Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail. Our study provides a structural blueprint for the neck and tail domains of myosin-1 and expands the target binding modes of the master Ca(2+)-signal regulator calmodulin.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Dev Cell. 2007 Sep;13(3):391-404 - PubMed
    1. Annu Rev Cell Dev Biol. 2011;27:133-55 - PubMed
    1. Nat Struct Biol. 1995 Sep;2(9):768-76 - PubMed
    1. Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501 - PubMed
    1. J Biol Chem. 1973 May 10;248(9):3313-26 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources