PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29725363-4 2018 Overexpression of CBP/PAG suppressed the growth of Jurkat cells by recruiting c-Src and its negative regulator, C-terminal Src kinase (CSK), to lipid rafts. phenylacetylglycine 22-25 C-terminal Src kinase Homo sapiens 112-133 29725363-4 2018 Overexpression of CBP/PAG suppressed the growth of Jurkat cells by recruiting c-Src and its negative regulator, C-terminal Src kinase (CSK), to lipid rafts. phenylacetylglycine 22-25 C-terminal Src kinase Homo sapiens 135-138 25897081-8 2015 In contrast, PTP1B potentiated SRC activity, but not by dephosphorylating SRC itself directly; instead, PTP1B regulated the interaction between CBP/PAG and CSK. phenylacetylglycine 148-151 C-terminal Src kinase Homo sapiens 156-159 25897081-9 2015 SRC associated with, and phosphorylated, the transmembrane protein CBP/PAG at Tyr-317, resulting in CSK recruitment. phenylacetylglycine 71-74 C-terminal Src kinase Homo sapiens 100-103 25897081-10 2015 We identified PAG as a substrate of PTP1B, and dephosphorylation abolished recruitment of the inhibitory kinase CSK. phenylacetylglycine 14-17 C-terminal Src kinase Homo sapiens 112-115 22659621-2 2012 In T cells, membrane docking of Csk is promoted by binding to FynT-phosphorylated Cbp/PAG (pTyr317) to allow targeting of substrates residing in lipid rafts. phenylacetylglycine 86-89 C-terminal Src kinase Homo sapiens 32-35 22777522-3 2012 We show that the hyperresponsive phenotype of B cells lacking Lyn is predicated on significantly increased basal and inducible PI3K activity that correlates with the constitutive hypophosphorylation of PAG/Cbp (phosphoprotein associated with glycosphingolipid-enriched microdomains/Csk-binding protein), a concomitant reduction in bound Csk in Lyn(-/-) B cells and elevated levels of active Fyn. phenylacetylglycine 202-205 C-terminal Src kinase Homo sapiens 282-285 20420835-4 2010 The A kinase anchoring protein Ezrin colocalizes PKA and Csk by forming a supramolecular signaling complex consisting of PKA, Ezrin, Ezrin/radixin/moesin (ERM) binding protein of 50 kDa (EBP50), phosphoprotein associated with glycosphingolipid-enriched membrane microdomains (GEMs) (PAG) and Csk. phenylacetylglycine 283-286 C-terminal Src kinase Homo sapiens 57-60 18491059-6 2008 One immunomodulating pathway is the cAMP-protein kinase A-Csk pathway scaffolded by a supramolecular complex residing in lipid rafts with the A kinase-anchoring protein (AKAP) ezrin, the Csk-binding protein PAG and a linker between the two, EBP50. phenylacetylglycine 207-210 C-terminal Src kinase Homo sapiens 58-61 18948260-7 2008 Finally, RPTPalpha-induced phosphorylation of Paxillin and Cbp/PAG induces recruitment of the SFK inhibitory kinase Csk, indicative of negative feedback loops limiting SFK activation by RPTPalpha. phenylacetylglycine 63-66 C-terminal Src kinase Homo sapiens 116-119 18721137-2 2008 Recruitment of Csk occurs via SH2-domain binding to PAG pTyr317, thus, the interaction is highly dependent on phosphorylation performed by the Src family kinase Fyn, which docks onto PAG using a dual-domain binding mode involving both SH3- and SH2-domains of Fyn. phenylacetylglycine 52-55 C-terminal Src kinase Homo sapiens 15-18 18721137-2 2008 Recruitment of Csk occurs via SH2-domain binding to PAG pTyr317, thus, the interaction is highly dependent on phosphorylation performed by the Src family kinase Fyn, which docks onto PAG using a dual-domain binding mode involving both SH3- and SH2-domains of Fyn. phenylacetylglycine 183-186 C-terminal Src kinase Homo sapiens 15-18 18085663-1 2008 PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases. phenylacetylglycine 0-3 C-terminal Src kinase Homo sapiens 141-162 18085663-1 2008 PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases. phenylacetylglycine 0-3 C-terminal Src kinase Homo sapiens 164-167 18085663-1 2008 PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases. phenylacetylglycine 0-3 C-terminal Src kinase Homo sapiens 192-195 18085663-5 2008 Despite being displaced, the mutant PAG molecule still binds the Src kinase Fyn and the cytoskeletal adaptor ezrin-radixin-moesin-binding phosphoprotein of 50 kDa, becomes tyrosine-phosphorylated, and recruits Csk to the membrane. phenylacetylglycine 36-39 C-terminal Src kinase Homo sapiens 210-213 18491059-6 2008 One immunomodulating pathway is the cAMP-protein kinase A-Csk pathway scaffolded by a supramolecular complex residing in lipid rafts with the A kinase-anchoring protein (AKAP) ezrin, the Csk-binding protein PAG and a linker between the two, EBP50. phenylacetylglycine 207-210 C-terminal Src kinase Homo sapiens 187-190 12665526-2 2003 Treatment of cells with the cAMP-elevating agent prostaglandin E(2) (PGE(2)) augmented the level of Cbp/PAG phosphorylation with a concomitant increase in amounts of Csk bound to Cbp/PAG. phenylacetylglycine 183-186 C-terminal Src kinase Homo sapiens 166-169 12612075-2 2003 In resting human T cells, PAG is tyrosine phosphorylated and associated with Csk, an inhibitor of Src-related protein tyrosine kinases. phenylacetylglycine 26-29 C-terminal Src kinase Homo sapiens 77-80 12612075-7 2003 By expressing wild-type and phosphorylation-defective (dominant-negative) PAG polypeptides in these cells, we found that the inhibitory effect of PAG is dependent on its capacity to be tyrosine phosphorylated and to associate with Csk. phenylacetylglycine 146-149 C-terminal Src kinase Homo sapiens 231-234 12612075-8 2003 PAG-mediated inhibition was accompanied by a repression of proximal TCR signaling and was rescued by expression of a constitutively activated Src-related kinase, implying that it is due to an inactivation of Src kinases by PAG-associated Csk. phenylacetylglycine 0-3 C-terminal Src kinase Homo sapiens 238-241 12612075-8 2003 PAG-mediated inhibition was accompanied by a repression of proximal TCR signaling and was rescued by expression of a constitutively activated Src-related kinase, implying that it is due to an inactivation of Src kinases by PAG-associated Csk. phenylacetylglycine 223-226 C-terminal Src kinase Homo sapiens 238-241 12612075-12 2003 Taken together, these data provide firm evidence that PAG is a bona fide negative regulator of T-cell activation as a result of its capacity to recruit Csk. phenylacetylglycine 54-57 C-terminal Src kinase Homo sapiens 152-155 12938237-6 2003 We also demonstrate that anti-CD4 treatment stimulated Csk kinase associated to the membrane adapter, PAG/Cbp, without affecting the total amount of Csk bound to PAG/Cbp. phenylacetylglycine 102-105 C-terminal Src kinase Homo sapiens 55-58 12665526-6 2003 Finally, raft-associated Csk already activated via Cbp/PAG binding, gained additional increase in phosphotransferase activity upon protein kinase A-mediated phosphorylation of Csk. phenylacetylglycine 55-58 C-terminal Src kinase Homo sapiens 25-28 11390365-1 2001 In resting peripheral T cells, Csk is constitutively present in lipid rafts through an interaction with the Csk SH2-binding protein, PAG, also known as Cbp. phenylacetylglycine 133-136 C-terminal Src kinase Homo sapiens 31-34 11390365-1 2001 In resting peripheral T cells, Csk is constitutively present in lipid rafts through an interaction with the Csk SH2-binding protein, PAG, also known as Cbp. phenylacetylglycine 133-136 C-terminal Src kinase Homo sapiens 108-111 11390365-3 2001 However, tyrosine phosphorylation of PAG/Cbp resumes after 3--5 min, at which time Csk reassociates with the rafts. phenylacetylglycine 37-40 C-terminal Src kinase Homo sapiens 83-86