| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| The incorporation of Rap 1b paralleled the incorporation of membrane glycoproteins ( GP ) IIb / IIIa and PECAM 1 , but not the incorporation of pp60c src . ^^^ |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| More important , SHP 2 bound not only PECAM 1 phosphopeptides , but also became associated with full length cellular PECAM 1 during the platelet aggregation process , and this interaction was mediated by the amino terminal Src homology 2 domains of the phosphatase . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| An autophosphorylatable band comigrating with c Src was co immunoprecipitated with anti PECAM 1 , and c Src phosphorylated and bound to a GST fusion protein containing the PECAM 1 cytoplasmic domain . ^^^ A spliced mRNA form lacking amino acid residues 703 721 in the cytoplasmic domain was also expressed in bovine ECs , c Src neither phosphorylated nor bound to the fusion protein containing the spliced PECAM 1 cytoplasmic domain which lacked one ( Tyr 713 ) of the six tyrosine residues in the PECAM 1 cytoplasmic domain . ^^^ Our study is the first demonstration of inducible tyrosine phosphorylation of PECAM 1 and suggests involvement of PECAM 1 and Src family kinases in the sensing / signal transduction of mechanical stimuli in ECs . . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| In addition , we identify the phosphorylation of a particular tyrosine residue in the PECAM 1 cytoplasmic domain , Tyr 686 , which has the potential of mediating binding to Src homology 2 domain containing proteins , affecting PECAM 1 cellular localization and endothelial cell migration . . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| PECAM 1 is more highly phosphorylated in endothelial cells overexpressing c Src , and in in vitro kinase assays , c Src can phosphorylate a glutathione S transferase ( GST ) PECAM cytoplasmic tail fusion protein . ^^^ The binding to the GST Src SH 2 affinity matrix correlates directly with the level of PECAM 1 phosphorylation , because more PECAM 1 is precipitated from c Src overexpressors and from wild type rather than Tyr 663 > Phe and Tyr 686 > Phe mutant PECAM 1 expressors . ^^^ We have previously noted that these two tyrosine residues are surrounded by consensus sequences for Src homology 2 ( SH 2 ) domain binding ( 1 , 2 ) , and the experiments presented explore the potential for PECAM 1 Src and PECAM 1 SH 2 domain interactions . ^^^ This association appears to be mediated by Src SH 2 domain , because PECAM 1 can be precipitated by a GST Src SH 2 affinity matrix . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| A 65 kDa protein from ECs specifically bound to the c Src phosphorylated PECAM 1 cytoplasmic domain and was identified as a protein tyrosine phosphatase SH PTP 2 ( SHP 2 , Syp ) . ^^^ |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Recent studies have shown that the Src homology 2 ( SH 2 ) domain containing protein tyrosine phosphatase , SHP 2 , associates with the cytoplasmic domain of PECAM 1 as it becomes tyrosine phosphorylated during platelet aggregation : a process that can be mimicked in part by small synthetic phosphopeptides corresponding to the cytoplasmic domain of PECAM 1 encompassing tyrosine residues Tyr 663 or Tyr 686 . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Regulation of mouse PECAM 1 tyrosine phosphorylation by the Src and Csk families of protein tyrosine kinases . ^^^ Furthermore , tyrosine phosphorylated PECAM 1 was shown to associate with SHP 2 , a Src homology 2 ( SH 2 ) domain containing protein tyrosine phosphatase expressed ubiquitously . ^^^ Through reconstitution experiments in COS 1 cells , we determined that mouse PECAM 1 could be tyrosine phosphorylated by Src related PTKs and Csk related PTKs , but not by other kinases such as Syk , Itk , and Pyk 2 . ^^^ Src related enzymes also phosphorylated mouse PECAM 1 at one or more yet to be identified sites . ^^^ In other studies , we demonstrated that phosphorylation of PECAM 1 by Src or Csk family kinases was sufficient to trigger its association with SHP 2 . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| We further show that the association of SHP 1 with PECAM 1 occurs through the direct interaction of the src homology region 2 domains of SHP 1 with two highly conserved phosphotyrosine binding motifs within PECAM 1 having the sequences NSDVQpY663TEVQV and DTETVpY686SEVRK ( where pY represents phosphotyrosine ) . ^^^ |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| The PECAM 1 cytoplasmic domain contains an immunoreceptor tyrosine based inhibitory motif ( ITIM ) that , when appropriately engaged , becomes phosphorylated on tyrosine residues , creating docking sites for nontransmembrane , Src homology 2 domain bearing protein tyrosine phosphatase ( SHP ) 1 and SHP 2 . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| We show here that , in thrombin stimulated human platelets , SHP 2 undergoes a time dependent association with platelet endothelial cell adhesion molecule 1 ( PECAM 1 ) and four low molecular weight phosphoproteins which are attenuated by the Src kinase inhibitor PP 1 . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| In PECAM 1 immunoprecipitates , Src family tyrosine kinases existed , and a kinase activity was detected , which increased upon WGA stimulation . ^^^ Our results suggest that ( 1 ) PECAM 1 is involved in WGA induced platelet activation , ( 2 ) PECAM 1 clustering by WGA activates unique and strong platelet signaling pathways , leading to a rapid PLC activation via Src family kinases , and ( 3 ) WGA is a useful tool for elucidating PECAM 1 mediated signaling with wide implications not confined to platelets . . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| The PECAM dependent H2O2 current was inhibited by dialysis of anti PECAM 1 cytoplasmic domain antibodies , required Src family tyrosine kinase activity , was independent of inositol trisphosphate receptor activation , and required only an intact PECAM 1 cytoplasmic domain . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Platelet endothelial cell adhesion molecule 1 ( PECAM 1 ) is a cell adhesion molecule with a cytoplasmic immunoreceptor tyrosine based inhibitory motif ( ITIM ) that , when phosphorylated , binds Src homology 2 domain containing protein tyrosine phosphatase ( SHP 2 ) . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Interestingly , LDL and the B site peptide also induce tyrosine phosphorylation of PECAM 1 , and studies with immunoprecipitates indicate the involvement of c Src . ^^^ |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Many of the regulatory functions of PECAM 1 are dependent on its tyrosine phosphorylation and subsequent recruitment of the Src homology ( SH 2 ) domain containing protein tyrosine phosphatase SHP 2 . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| This was consistent with increased amounts of Src and SHP 2 associated with PECAM 1 , and enhanced migration and proliferation in TSP 1 / retinal EC . ^^^ |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| PECAM 1 ( / ) neutrophils also exhibited intracellularly dislocalized Src homology 2 domain containing phosphatase 1 ( SHP 1 ) and had less IL 8 induced SHP 1 phosphatase activity . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Src , SHP 2 , and alternative PECAM 1 pre mRNA splicing play a regulatory role in these signaling events . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| Src homology 2 domain containing phosphatase 2 ( SHP 2 ) association with beta catenin was diminished in PECAM 1 null ECs , suggesting that lack of PECAM 1 inhibits the ability of this adherens junction component to become dephosphorylated , promoting a sustained increase in permeability . beta Catenin / Glycogen synthase kinase 3 ( GSK 3beta ) association and beta catenin serine phosphorylation levels were increased and beta catenin expression levels were reduced in PECAM 1 null ECs . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| CD 31 tyrosine phosphorylation was reduced or abolished by the Src family kinase inhibitor PP 2 , suggesting a role for these enzymes . ^^^ In accordance with this , each of the Src family members expressed in platelets , namely Fyn , Lyn , Src , Yes , and Hck , was shown to co immunoprecipitate with CD 31 . ^^^ |
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| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| METHODS : Reverse transcriptase polymerase chain reaction ( RT PCR ) coupled with Southern blot analysis was used to derive a semiquantitative estimate of the relative levels of SRC 1 , SRC 2 , and SRC 3 expression in pure populations of SMC ( > 98 % alpha smooth muscle actin [ SMA ] ( + ) ) and MEC ( > 99 % CD 31 ( + ) ) isolated and cultured from eight samples of paired human myometrial and fibroid tissue . ^^^ |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P16284 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
|