Calmodulin-like protein enhances myosin-10 translation

Richard D. Bennett, Emanuel E. Strehler

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Myosin-10 (Myo10) is involved in processes ranging from filopodial formation and extension to spindle orientation during cell division. Myo10 contains three IQ motifs that bind calmodulin and calmodulin-like protein (CLP) as light chains. We recently found that CLP expression up-regulates Myo10, leading to increased Myo10-dependent cell motility and filopodial extension [R.D. Bennett, et al., J. Biol. Chem. 282 (2007) 3205-3212]. CLP-dependent Myo10 up-regulation occurs without increase in Myo10 mRNA. We followed Myo10 degradation in vivo and in vitro and found that it was unaffected by CLP. Myo10 decayed rapidly with a half-life of ∼2.5 h. Using an in vitro transcription/translation system we determined that CLP increased Myo10 translation, resulting in a higher relative accumulation of Myo10 in the presence than in the absence of CLP. Our data suggest that CLP functions to increase translation of Myo10 possibly by acting as a chaperone for the emerging Myo10 heavy chain protein.

Original languageEnglish (US)
Pages (from-to)654-659
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume369
Issue number2
DOIs
StatePublished - May 2 2008

Keywords

  • Calmodulin-like protein
  • Chaperone
  • IQ motif
  • In vitro translation
  • Myosin light chain
  • Myosin-10

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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