title: Calmodulin-like protein enhances myosin-10 translation.
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 approximately 2.5h. 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, 200 First Street S.W., Rochester, MN 55905, USA; Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN, USA.
authors.forename: Richard D
authors.initials: RD
authors.lastname: Bennett
authors.forename: Emanuel E
authors.initials: EE
authors.lastname: Strehler
mesh_terms: D002147:Calmodulin / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D009218:Myosins / Q000378:metabolism*; D046188:Protein Modification, Translational / Q000502:physiology*
chemical_list: C082965:CALML3 protein, human; D002147:Calmodulin; C498718:MYO10 protein, human; D009218:Myosins