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

Richard D. Bennett, Ariel J. Caride, Amy S. Mauer, Emanuel E. Strehler

Research output: Contribution to journalArticle

6 Scopus citations

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).

Original languageEnglish (US)
Pages (from-to)2377-2381
Number of pages5
JournalFEBS Letters
Volume582
Issue number16
DOIs
StatePublished - Jul 9 2008

Keywords

  • Calmodulin-like protein
  • Filopodia
  • IQ domain
  • Motility
  • Myosin-10

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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