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Effect of Mts1 on the Structure and Activity of Nonmuscle Myosin II

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Department of Biochemistry and Cancer Center, University of Rochester, 601 Elmwood Avenue, Rochester, New York 14642, Laboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892, and Laboratory of Cellular Biology, National Institute on Deafness and Other Communication Disorders, Bethesda, Maryland 20892
Cite this: Biochemistry 1997, 36, 51, 16321–16327
Publication Date (Web):December 23, 1997
https://doi.org/10.1021/bi971182l
Copyright © 1997 American Chemical Society

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    Abstract

    The mts1 gene codes for a 9 kDa protein belonging to the S100 subfamily of Ca2+-binding proteins and is known to play a role in metastasis. Its role in metastasis may be through cellular locomotion, as transfection of mts1 into mouse mammary adenocarcinoma cells increases cellular motility in modified Boyden chemotaxis chambers. The Mts1 protein interacts with nonmuscle myosin II in the presence of Ca2+ with an affinity of approximately 7.9 × 104 M-1 and an approximate stoichiometry of 3 mol of Mts1/mol of myosin heavy chain. No interaction was found with myosin I or myosin V. The binding site of Mts1 on myosin is in the rod region, particularly to the light meromyosin portion of the rod. To understand the mechanism by which Mts1 alters cellular motility, we examined its effect on myosin structure and activity. Cosedimentation analysis and electron microscopy suggest that Mts1 destabilizes myosin filaments. In the presence of Ca2+, Mts1 inhibits the actin-activated MgATPase activity of myosin in vitro. The data demonstrate an effect of Mts1 on both myosin structure and function, and suggest a route through which Mts1 affects motility as well as metastasis.

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     Research was supported by NIH Cancer Center Core Grant P30CA11198 and by NIH Grant R01CA62376 to S.B.Z. H.L.F. has been supported as a trainee on the NRSA Genetics and Regulation Training Grant and on the Elon Huntington Hooker Graduate Fellowship.

    *

     Author to whom correspondance should be addressed.

     Department of Biochemistry, University of Rochester.

    §

     Present address:  Dana-Farber Cancer Institute, Room D810B, 44 Binney St., Boston, MA 02115. Telephone:  (617) 632-4686. Fax:  (617) 632-4680.

     National Heart, Lung, and Blood Institute.

     National Institute on Deafness and Other Communication Disorders.

    #

     Cancer Center, University of Rochester.

     Abstract published in Advance ACS Abstracts, December 1, 1997.

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