Document Detail


Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10.
MedLine Citation:
PMID:  17130134     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human calmodulin-like protein (CLP) is an epithelial-specific protein that is expressed during cell differentiation but down-regulated in primary cancers and transformed cell lines. Using stably transfected and inducible HeLa cell lines, we found that CLP expression did not alter the proliferation rate and colony-forming potential of these cells. However, remarkable phenotypic changes were observed in CLP-expressing compared with control cells. Soft agar colonies of CLP-expressing cells had rough boundaries, with peripheral cells migrating away from the colony. Cells expressing CLP displayed a striking increase in the number and length of myosin-10-positive filopodia and showed increased mobility in a wound healing assay. This increase in wound healing capacity was prevented by small interference RNA-mediated down-regulation of myosin-10. Fluorescence microscopy and Western blotting revealed that CLP expression results in up-regulation of its target protein, myosin-10. This up-regulation occurs at the protein level by stabilization of myosin-10. Thus, CLP functions by increasing the stability of myosin-10, leading to enhanced myosin-10 function and a subsequent increase in filopodial dynamics and cell migration. In stratified epithelia, CLP may be required during terminal differentiation to increase myosin-10 function as cells migrate toward the upper layers and establish new adhesive contacts.
Authors:
Richard D Bennett; Amy S Mauer; Emanuel E Strehler
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-11-26
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  282     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-01-29     Completed Date:  2007-04-10     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3205-12     Citation Subset:  IM    
Affiliation:
Cell Biology and Genetics Program, Mayo Graduate School, Mayo Clinic College of Medicine, Minnesota 55905, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Base Sequence
Calmodulin / genetics,  physiology*
Cell Division
Cell Movement / physiology*
DNA Primers
Hela Cells
Humans
Molecular Sequence Data
Myosins / genetics,  metabolism*
Peptide Fragments / chemistry
Pseudopodia / physiology*
Reverse Transcriptase Polymerase Chain Reaction
Transfection
Chemical
Reg. No./Substance:
0/CALML3 protein, human; 0/Calmodulin; 0/DNA Primers; 0/MYO10 protein, human; 0/Peptide Fragments; EC 3.6.4.1/Myosins

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