|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
2004-4-19
|
|
pubmed:abstractText |
The precise biological role of Thy-1, a glycophosphatidyl-inositol (GPI)-linked cell surface glycoprotein in non-caveolar lipid raft microdomains, remains enigmatic. Evidence suggests that Thy-1 affects intracellular signaling through src-family protein kinases, and modulates adhesive and migratory events, such as thymocyte adhesion and neurite extension. Primary fibroblasts sorted based on presence or absence of cell surface Thy-1 display strikingly distinct morphologies and differ with respect to production of and response to cytokines and growth factors. It is unclear the extent to which Thy-1 mediates these differences. Findings reported here indicate a novel role for Thy-1 in regulating the activity of Rho GTPase, a critical regulator of cellular adhesion and cytoskeletal organization. Endogenous or heterologous Thy-1 expression promotes focal adhesion and stress fiber formation, characteristic of increased Rho GTPase activity, and inhibits migration. Immunoblotting following transfection of RFL6 fibroblasts with Thy-1 demonstrates that Thy-1 expression inhibits src-family protein tyrosine kinase (SFK) activation, resulting in decreased phosphorylation of p190 Rho GTPase-activating protein (GAP). This results in a net increase in active Rho, and increased stress fibers and focal adhesions. We therefore conclude that Thy-1 surface expression regulates fibroblast focal adhesions, cytoskeletal organization and migration by modulating the activity of p190 RhoGAP and Rho GTPase.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Thy-1,
http://linkedlifedata.com/resource/pubmed/chemical/Arhgap5 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Grlf1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Grlf1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
May
|
|
pubmed:issn |
0014-4827
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
295
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
488-96
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:15093746-Animals,
pubmed-meshheading:15093746-Antigens, Thy-1,
pubmed-meshheading:15093746-Cell Movement,
pubmed-meshheading:15093746-Cells, Cultured,
pubmed-meshheading:15093746-Cytoskeleton,
pubmed-meshheading:15093746-DNA-Binding Proteins,
pubmed-meshheading:15093746-Enzyme Activation,
pubmed-meshheading:15093746-Fibroblasts,
pubmed-meshheading:15093746-Focal Adhesions,
pubmed-meshheading:15093746-GTPase-Activating Proteins,
pubmed-meshheading:15093746-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:15093746-Lung,
pubmed-meshheading:15093746-Mice,
pubmed-meshheading:15093746-Mice, Knockout,
pubmed-meshheading:15093746-Models, Biological,
pubmed-meshheading:15093746-Nuclear Proteins,
pubmed-meshheading:15093746-Phosphorylation,
pubmed-meshheading:15093746-Protein-Tyrosine Kinases,
pubmed-meshheading:15093746-Rats,
pubmed-meshheading:15093746-Rats, Inbred Lew,
pubmed-meshheading:15093746-Repressor Proteins,
pubmed-meshheading:15093746-rho GTP-Binding Proteins,
pubmed-meshheading:15093746-src-Family Kinases
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
Thy-1 regulates fibroblast focal adhesions, cytoskeletal organization and migration through modulation of p190 RhoGAP and Rho GTPase activity.
|
|
pubmed:affiliation |
Department of Medicine, The University of Alabama at Birmingham, Birmingham, AL 35294, USA.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|
