Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-5-9
pubmed:abstractText
Rsu-1 is a highly conserved leucine rich repeat (LRR) protein that is expressed ubiquitously in mammalian cells. Rsu-1 was identified based on its ability to inhibit transformation by Ras, and previous studies demonstrated that ectopic expression of Rsu-1 inhibited anchorage-independent growth of Ras-transformed cells and human tumor cell lines. Using GAL4-based yeast two-hybrid screening, the LIM domain protein, PINCH1, was identified as the binding partner of Rsu-1. PINCH1 is an adaptor protein that localizes to focal adhesions and it has been implicated in the regulation of adhesion functions. Subdomain mapping in yeast revealed that Rsu-1 binds to the LIM 5 domain of PINCH1, a region not previously identified as a specific binding domain for any other protein. Additional testing demonstrated that PINCH2, which is highly homologous to PINCH1, except in the LIM 5 domain, does not interact with Rsu-1. Glutathione transferase fusion protein binding studies determined that the LRR region of Rsu-1 interacts with PINCH1. Transient expression studies using epitope-tagged Rsu-1 and PINCH1 revealed that Rsu-1 co-immunoprecipitated with PINCH1 and colocalized with vinculin at sites of focal adhesions in mammalian cells. In addition, endogenous P33 Rsu-1 from 293T cells co-immunoprecipitated with transiently expressed myc-tagged PINCH1. Furthermore, RNAi-induced reduction in Rsu-1 RNA and protein inhibited cell attachment, and while previous studies demonstrated that ectopic expression of Rsu-1 inhibited Jun kinase activation, the depletion of Rsu-1 resulted in activation of Jun and p38 stress kinases. These studies demonstrate that Rsu-1 interacts with PINCH1 in mammalian cells and functions, in part, by altering cell adhesion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein..., http://linkedlifedata.com/resource/pubmed/chemical/LIM Domain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Lims1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering, http://linkedlifedata.com/resource/pubmed/chemical/Rsu1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Vinculin, http://linkedlifedata.com/resource/pubmed/chemical/leucine-rich repeat proteins, http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein...
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
306
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
168-79
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:15878342-Adaptor Proteins, Signal Transducing, pubmed-meshheading:15878342-Animals, pubmed-meshheading:15878342-Binding Sites, pubmed-meshheading:15878342-COS Cells, pubmed-meshheading:15878342-Cell Adhesion, pubmed-meshheading:15878342-Cell Line, pubmed-meshheading:15878342-Cercopithecus aethiops, pubmed-meshheading:15878342-DNA-Binding Proteins, pubmed-meshheading:15878342-Focal Adhesions, pubmed-meshheading:15878342-Humans, pubmed-meshheading:15878342-Immunoprecipitation, pubmed-meshheading:15878342-JNK Mitogen-Activated Protein Kinases, pubmed-meshheading:15878342-LIM Domain Proteins, pubmed-meshheading:15878342-Membrane Proteins, pubmed-meshheading:15878342-Mice, pubmed-meshheading:15878342-Mutation, pubmed-meshheading:15878342-Protein Binding, pubmed-meshheading:15878342-Proteins, pubmed-meshheading:15878342-RNA, Small Interfering, pubmed-meshheading:15878342-Saccharomyces cerevisiae, pubmed-meshheading:15878342-Transcription Factors, pubmed-meshheading:15878342-Transfection, pubmed-meshheading:15878342-Two-Hybrid System Techniques, pubmed-meshheading:15878342-Vinculin, pubmed-meshheading:15878342-p38 Mitogen-Activated Protein Kinases
pubmed:year
2005
pubmed:articleTitle
The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions.
pubmed:affiliation
Department of Pathology, Uniformed Services University of the Health Sciences, 4301 Jones Bridge Road, B3122, Bethesda, MD 20814, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't