Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-5-25
pubmed:databankReference
pubmed:abstractText
Tensin is a cytoskeletal protein that links integrins to the actin cytoskeleton at sites of cell-matrix adhesion. Here we describe the crystal structure of the phosphotyrosine-binding (PTB) domain of tensin1, and show that it binds integrins in an NPxY-dependent fashion. Alanine mutagenesis of both the PTB domain and integrin tails supports a model of integrin binding similar to that of the PTB-like domain of talin. However, we also show that phosphorylation of the NPxY tyrosine, which disrupts talin binding, has a negligible effect on tensin binding. This suggests that tyrosine phosphorylation of integrin, which occurs during the maturation of focal adhesions, could act as a switch to promote the migration of tensin-integrin complexes into fibronectin-mediated fibrillar adhesions.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-10089316, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-10318759, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-10497155, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-10704455, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-10712519, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-10747019, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-11090629, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-11493667, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-11792844, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-11932255, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12154022, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12230976, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12297042, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12495434, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12535520, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12606711, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12737822, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-12906822, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-14500982, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-14526080, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-14576354, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-14593208, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-14607833, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-14691141, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-15140944, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-15378069, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-17218263, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-2468126, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-7896874, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-8195290, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-8524391, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-8599766, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-8646778, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-8798552, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-9321393, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-9757107, http://linkedlifedata.com/resource/pubmed/commentcorrection/17473008-9846878
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0961-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1223-9
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions.
pubmed:affiliation
Cancer Center, Burnham Institute for Medical Research, La Jolla, California 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural