Document Detail


Scapinin, the protein phosphatase 1 binding protein, enhances cell spreading and motility by interacting with the actin cytoskeleton.
MedLine Citation:
PMID:  19158953     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Scapinin, also named phactr3, is an actin and protein phosphatase 1 (PP1) binding protein, which is expressed in the adult brain and some tumor cells. At present, the role(s) of scapinin in the brain and tumors are poorly understood. We show that the RPEL-repeat domain of scapinin, which is responsible for its direct interaction with actin, inhibits actin polymerization in vitro. Next, we established a Hela cell line, where scapinin expression was induced by tetracycline. In these cells, expression of scapinin stimulated cell spreading and motility. Scapinin was colocalized with actin at the edge of spreading cells. To explore the roles of the RPEL-repeat and PP1-binding domains, we expressed wild-type and mutant scapinins as fusion proteins with green fluorescence protein (GFP) in Cos7 cells. Expression of GFP-scapinin (wild type) also stimulated cell spreading, but mutation in the RPEL-repeat domain abolished both the actin binding and the cell spreading activity. PP1-binding deficient mutants strongly induced cell retraction. Long and branched cytoplasmic processes were developed during the cell retraction. These results suggest that scapinin enhances cell spreading and motility through direct interaction with actin and that PP1 plays a regulatory role in scapinin-induced morphological changes.
Authors:
Junji Sagara; Toshiaki Arata; Shunichiro Taniguchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-01-22
Journal Detail:
Title:  PloS one     Volume:  4     ISSN:  1932-6203     ISO Abbreviation:  PLoS ONE     Publication Date:  2009  
Date Detail:
Created Date:  2009-01-22     Completed Date:  2009-04-14     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  101285081     Medline TA:  PLoS One     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e4247     Citation Subset:  IM    
Affiliation:
Department of Biomedical Laboratory Sciences, School of Health Sciences, Shinshu University, Matsumoto, Nagano, Japan. sagaraj@shinshu-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Actins / chemistry*
Amino Acid Sequence
Animals
COS Cells
Cell Movement
Cercopithecus aethiops
Cytoskeleton / metabolism*
HeLa Cells
Humans
Molecular Sequence Data
Mutation
Nuclear Proteins / chemistry*,  physiology*
Protein Binding
Protein Phosphatase 1 / metabolism*
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Actins; 0/Nuclear Proteins; 0/PHACTR3 protein, human; EC 3.1.3.16/Protein Phosphatase 1
Comments/Corrections

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