Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
Inhibition of protein tyrosine phosphatase 1B abrogated cAMP mediated disruption of actin cytoskeleton , cav 1 phosphorylation , and FAK Tyr 397 dephosphorylation . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
Time course experiments in both spreading and aggregated platelets revealed that talin , FAK , and PTP 1B were proteolyzed after translocation to the cytoskeleton . ^^^ The activation of calpain in both spreading and aggregated platelets resulted in a substantial decrease in the level of tyrosine phosphorylation of multiple platelet proteins and was associated with a 50 80 % reduction in the amount of cytoskeletal associated talin , integrin alphaIIbbeta 3 , PI 3 kinase , FAK , pp 60 ( c ) src , and PTP 1B . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
To explore the cellular mechanism whereby TNF alpha regulates phosphorylation of FAK in the liver , we measured c Src kinase activity and the abundance of 3 major protein tyrosine phosphatases ( PTPs ) ( PTP 1B , leukocyte antigen related tyrosine phosphatase [ LAR ] , and src homology 2 domain containing protein tyrosine phosphatase [ SHPTP 2 ] ) in liver homogenates from obese Zucker rats after TNF alpha blockade . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
The altered regulation of PTP 1B and SHP 2 in kidneys from bcl 2 / mice correlates with sustained phosphorylation of FAK and paxillin . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
Furthermore , we show that coexpression of wild type alpha actinin and PTP 1B causes dephosphorylation at Tyr 397 in FAK . ^^^ Furthermore , the phosphorylation at four other sites in FAK was not altered by PTP 1B . ^^^ The dephosphorylation at Tyr 397 in FAK triggered by wild type alpha actinin and PTP 1B caused a significant increase in cell migration . ^^^ We propose that phosphorylated alpha actinin disrupts the FAK 10 Src complex exposing Tyr 397 in FAK to PTP 1B . ^^^ These findings uncover a novel feedback loop involving phosphorylated alpha actinin and PTP 1B that regulates FAK 10 Src interaction and cell migration . . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
Attachment to fibronectin induces tyrosine phosphorylation of focal adhesion kinase ( FAK ) and paxillin in parental cells and cells transfected with the wild type PTP1B , while in cells transfected with the mutant PTP1B , such induction is not observed . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
Cas transmits signals through interactions with the Src homology 3 ( SH 3 ) and Src homology 2 domains of FAK or 5 Crk signaling molecules , or with 14 3 3 protein , as well as phosphatases PTP1B and PTP PEST . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
The SH 3 domain of CAS mediates its interaction with several proteins involved in signaling pathways such as focal adhesion kinase ( FAK ) , tyrosine phosphatases PTP1B and PTP PEST , and the guanine nucleotide exchange factor C3G . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
We show that down regulation of PTP1B activity with small molecule inhibitors suppresses cell spreading and migration to fibronectin , increases Tyr ( 527 ) phosphorylation in Src , and decreases phosphorylation of FAK , p 130 ( Cas ) , and ERK1 / 2 . ^^^
Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
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Interacting proteins: P18031 and Q05397 Pubmed SVM Score :0.0
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