FEBS Letters
Volume 582, Issue 16 , Pages 2377-2381, 9 July 2008

Interaction with the IQ3 motif of myosin-10 is required for calmodulin-like protein-dependent filopodial extension

Edited by Berend Wieringa

  • Richard D. Bennett

      Affiliations

    • Cell Biology and Genetics Program, Mayo Graduate School, Rochester, MN 55905, USA
    • Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street S.W., Rochester, MN 55905, USA
    • Current address: McLaughlin Research Institute, Great Falls, MT 59405, USA.
    • ,
  • Ariel J. Caride

      Affiliations

    • Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street S.W., Rochester, MN 55905, USA
    • ,
  • Amy S. Mauer

      Affiliations

    • Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street S.W., Rochester, MN 55905, USA
    • ,
  • Emanuel E. Strehler

      Affiliations

    • Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street S.W., Rochester, MN 55905, USA
    • Corresponding Author InformationCorresponding author. Fax: +1 507 284 2384.

Received 8 February 2008; received in revised form 25 April 2008; accepted 20 May 2008. published online 19 June 2008.

Abstract 

Calmodulin-like protein (CLP) is a specific light chain of unconventional myosin-10 (Myo10) and enhances Myo10-dependent filopodial extension. Here we show that phenylalanine-795 in the third IQ domain (IQ3) of Myo10 is critical for CLP binding. Remarkably, mutation of F795 to alanine had little effect on calmodulin binding to IQ3. Fluorescence microscopy and time-lapse video microscopy showed that HeLa cells expressing CLP and transiently transfected with GFP-Myo10-F795A exhibited significantly shorter filopodia and decreased intrafilopodial motility compared to wildtype GFP-Myo10-transfected cells. Thus, F795 represents a unique anchor for CLP and is essential for CLP-mediated Myo10 function in filopodial extension and motility.

Structured summary


MINT-6595901: GST-IQ3 Myo10 (uniprotkb:Q9HD67) binds (MI:0407) to CLP (uniprotkb:P27482) by pull down (MI:0096)

MINT-6596000: CLP (uniprotkb:P27482) and GST-IQ3 Myo10 (uniprotkb:Q9HD67) bind (MI:0407) by classical fluorescence spectroscopy (MI:0017)

MINT-6596013: CaM (uniprotkb:P62158) and GST-IQ3 Myo10 (uniprotkb:Q9HD67) bind (MI:0407) by classical fluorescence spectroscopy (MI:0017)

MINT-6595938:GST-IQ3 Myo10 (uniprotkb:Q9HD67) binds (MI:0407) to CaM (uniprotkb:P62158) by pull down (MI:0096)

Abbreviations: CaM, calmodulin, CLP, calmodulin-like protein, GST, glutathione S-transferase, Myo10, myosin-10, TA-CaM, 2-chloro-(ε-amino-Lys75)-[6-[4-(N,N-diethylamino)phenyl]-1,3,5-triazin-4-yl]calmodulin

Keywords: Calmodulin-like protein, Filopodia, IQ domain, Motility, Myosin-10

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PII: S0014-5793(08)00502-4

doi:10.1016/j.febslet.2008.05.051

FEBS Letters
Volume 582, Issue 16 , Pages 2377-2381, 9 July 2008

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