Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2006-6-16
pubmed:abstractText
Ena/VASP family proteins are important modulators of cell migration and localize to focal adhesions, stress fibres and the very tips of lamellipodia and filopodia. Proline-rich proteins like vinculin and zyxin are well established interaction partners, which mediate Ena/VASP-recruitment via their EVH1-domains to focal adhesions and stress fibres. However, it is still unclear, which binding partners Ena/VASP proteins may have at lamellipodia tips and how their recruitment to these cellular protrusions is regulated. Here, we report the identification of a novel protein with high similarity to the C. elegans MIG-10 protein, which we termed PREL1 (Proline Rich EVH1 Ligand). PREL1 is a 74 kDa protein and shares homology with the Grb7-family of signalling adaptors. We show that PREL1 directly binds to Ena/VASP proteins and co-localizes with them at lamellipodia tips and at focal adhesions in response to Ras activation. Moreover, PREL1 directly binds to activated Ras in a phosphoinositide-dependent manner. Thus, our data pinpoint PREL1 as the first direct link between Ras signalling and cytoskeletal remodelling via Ena/VASP proteins during cell migration and spreading.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/APBB1IP protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Vinculin, http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins, http://linkedlifedata.com/resource/pubmed/chemical/vasodilator-stimulated...
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
580
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
455-63
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:16783873-Actin Cytoskeleton, pubmed-meshheading:16783873-Actins, pubmed-meshheading:16783873-Adaptor Proteins, Signal Transducing, pubmed-meshheading:16783873-Animals, pubmed-meshheading:16783873-Antibodies, Monoclonal, pubmed-meshheading:16783873-Biological Assay, pubmed-meshheading:16783873-Cell Adhesion, pubmed-meshheading:16783873-Cell Adhesion Molecules, pubmed-meshheading:16783873-Cell Line, pubmed-meshheading:16783873-Cell Movement, pubmed-meshheading:16783873-Cytoskeletal Proteins, pubmed-meshheading:16783873-DNA-Binding Proteins, pubmed-meshheading:16783873-Fibroblasts, pubmed-meshheading:16783873-Fibronectins, pubmed-meshheading:16783873-Glycoproteins, pubmed-meshheading:16783873-Humans, pubmed-meshheading:16783873-Immunoprecipitation, pubmed-meshheading:16783873-Membrane Proteins, pubmed-meshheading:16783873-Mice, pubmed-meshheading:16783873-Microfilament Proteins, pubmed-meshheading:16783873-Phosphoproteins, pubmed-meshheading:16783873-Pseudopodia, pubmed-meshheading:16783873-Signal Transduction, pubmed-meshheading:16783873-Vinculin, pubmed-meshheading:16783873-ras Proteins
pubmed:year
2006
pubmed:articleTitle
PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins.
pubmed:affiliation
Department of Cell Biology, German Research Centre for Biotechnology (GBF), Braunschweig, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Duplicate Publication