PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11007954-5 2000 By means of its SH3 domains, Grb2 recognizes proline-rich sequences of Sos, leading to Ras activation. Proline 45-52 growth factor receptor bound protein 2 Homo sapiens 29-33 10903901-1 2000 The beta-dystroglycan/Grb2 interaction was investigated and a proline-rich region within beta-dystroglycan that binds Grb2-src homology 3 domains identified. Proline 62-69 growth factor receptor bound protein 2 Homo sapiens 118-122 10869177-0 2000 Circular dichroic investigation of the native and non-native conformational states of the growth factor receptor-binding protein 2 N-terminal src homology domain 3: effect of binding to a proline-rich peptide from guanine nucleotide exchange factor. Proline 188-195 growth factor receptor bound protein 2 Homo sapiens 90-130 10749687-12 2000 With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Proline 160-167 growth factor receptor bound protein 2 Homo sapiens 78-82 10747847-5 2000 A central proline-rich motif associated with the Src homology (SH)2/SH3-containing adapter proteins Grb2 and Nck in vivo, whereas a pleckstrin homology (PH) domain was located at the GEF C terminus. Proline 10-17 growth factor receptor bound protein 2 Homo sapiens 100-104 10749687-12 2000 With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Proline 160-167 growth factor receptor bound protein 2 Homo sapiens 92-96 10749687-12 2000 With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Proline 160-167 growth factor receptor bound protein 2 Homo sapiens 92-96 10749687-12 2000 With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Proline 160-167 growth factor receptor bound protein 2 Homo sapiens 92-96 10395825-8 1999 Finally, the affinity of the proline-rich peptide GPPPQVPSRPNR, derived from dynamin, for the Grb2 N-SH3 domain was too low to be analyzed by NMR. Proline 29-36 growth factor receptor bound protein 2 Homo sapiens 94-98 10636929-5 2000 Second, the Itk proline-rich region binds to Grb2 and LAT. Proline 16-23 growth factor receptor bound protein 2 Homo sapiens 45-49 10393272-2 1999 The major function of these adaptors, such as Grb2, Nck, and Crk, is to recruit proline-rich effector molecules to tyrosine-phosphorylated kinases or their substrates. Proline 80-87 growth factor receptor bound protein 2 Homo sapiens 46-50 9891069-3 1999 We found that HPK1 interacted with Crk and CrkL adaptor proteins in vitro and in vivo and that the proline-rich motifs within HPK1 were involved in the differential interaction of HPK1 with the Crk proteins and Grb2. Proline 99-106 growth factor receptor bound protein 2 Homo sapiens 211-215 12054111-7 1999 The carboxyl terminal domain of SOS contains a proline-rich regions that directs its association with the SH3 domains of the small adapter protein, Grb2. Proline 47-54 growth factor receptor bound protein 2 Homo sapiens 148-152 9388224-8 1997 Protein binding assays demonstrated that among the major src homology 3-proteins known to bind to the proline-rich region of synaptojanin 1, Grb2, amphiphysin, and members of SH3p4/8/13 protein family, only Grb2 bound to that of synaptojanin 2. Proline 102-109 growth factor receptor bound protein 2 Homo sapiens 141-145 9694876-0 1998 Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction. Proline 82-89 growth factor receptor bound protein 2 Homo sapiens 0-4 9516488-9 1998 However, although the proline-rich motif of hnRNP C is involved in the interaction with Grb2, it is not in the binding to Grb3-3. Proline 22-29 growth factor receptor bound protein 2 Homo sapiens 88-92 9569023-4 1998 The proline-rich sequences of Sos mediate the interaction of Sos with Grb2, an adaptor protein which coupled tyrosine kinase receptors to Sos. Proline 4-11 growth factor receptor bound protein 2 Homo sapiens 70-74 9569023-8 1998 Proline-rich peptides corresponding to Dab2 (#661-669) and to Sos (#1146-1161) inhibited the binding of Dab2 to Grb2, but were less effective in disrupting the Grb2-Sos complex. Proline 0-7 growth factor receptor bound protein 2 Homo sapiens 112-116 9569023-8 1998 Proline-rich peptides corresponding to Dab2 (#661-669) and to Sos (#1146-1161) inhibited the binding of Dab2 to Grb2, but were less effective in disrupting the Grb2-Sos complex. Proline 0-7 growth factor receptor bound protein 2 Homo sapiens 160-164 9569023-9 1998 The expressed proline-rich domain of Dab2 (#600-730) bound Grb2, but other regions of Dab2 failed to bind Grb2. Proline 14-21 growth factor receptor bound protein 2 Homo sapiens 59-63 9569023-11 1998 These data indicate that Dab2 binds to the SH3 domains of Grb2 via its C-terminal proline-rich sequences. Proline 82-89 growth factor receptor bound protein 2 Homo sapiens 58-62 9484780-3 1998 Grb2 binds proline-rich motifs in Shb via its SH3 domains. Proline 11-18 growth factor receptor bound protein 2 Homo sapiens 0-4 9452513-3 1998 Microtubules and Grb2 bind to the carboxyl-terminal proline/arginine-rich domain (PRD), whereas phosphoinositides bind to the pleckstrin homology (PH) domain. Proline 52-59 growth factor receptor bound protein 2 Homo sapiens 17-21 9388224-8 1997 Protein binding assays demonstrated that among the major src homology 3-proteins known to bind to the proline-rich region of synaptojanin 1, Grb2, amphiphysin, and members of SH3p4/8/13 protein family, only Grb2 bound to that of synaptojanin 2. Proline 102-109 growth factor receptor bound protein 2 Homo sapiens 207-211 9346925-6 1997 The SH3 domains of Grb2 bound in vitro to specific proline-rich motifs in the HPK1 tail and functioned synergistically to direct the stable binding of Grb2 to HPK1 in transfected Cos1 cells. Proline 51-58 growth factor receptor bound protein 2 Homo sapiens 19-23 9344857-3 1997 A novel molecule detected therefrom (referred to as Nck-, Ash- and phospholipase Cgamma-binding protein 4) contained proline-rich sequences and, through the function of one of them, interacted with the middle SH3 domain of Nck. Proline 117-124 growth factor receptor bound protein 2 Homo sapiens 58-61 7592693-9 1995 Both Grb2 and EGF receptors are released from Cbl in the presence of a proline-rich peptide that binds the NH2-terminal SH3 domain of Grb2. Proline 71-78 growth factor receptor bound protein 2 Homo sapiens 5-9 9108392-3 1997 These domains bind to proteins containing proline-rich regions or tyrosine-phosphorylated proteins and contribute to the association of Grb2/Ash and Shc with other signaling molecules. Proline 42-49 growth factor receptor bound protein 2 Homo sapiens 136-140 9108392-3 1997 These domains bind to proteins containing proline-rich regions or tyrosine-phosphorylated proteins and contribute to the association of Grb2/Ash and Shc with other signaling molecules. Proline 42-49 growth factor receptor bound protein 2 Homo sapiens 141-144 8985255-7 1997 Formation of this intramolecular SH3-ligand complex prevents the Itk SH3 domain and proline-rich region from interacting with their respective protein ligands, Sam68 and Grb-2. Proline 84-91 growth factor receptor bound protein 2 Homo sapiens 170-175 8824292-8 1996 Additionally, we used truncation mutations of p120(cbl) to map the p120(cbl)-Grb2 interaction to amino acids 481-528 of p120(cbl); this interaction is stronger in longer constructs that include additional proline-rich motifs. Proline 205-212 growth factor receptor bound protein 2 Homo sapiens 77-81 8663276-8 1996 Mutation of the ICP10 proline-rich motifs at positions 396 and 149 reduced Grb2 binding 20- and 2-fold, respectively. Proline 22-29 growth factor receptor bound protein 2 Homo sapiens 75-79 8670803-5 1996 The inclusion of peptides encompassing an hSos1 proline-rich motif in cell lysates resulted in enhanced binding of RPTPalpha to GRB2 in vitro, suggesting that steric hindrance prohibits formation of the RPTPalpha-GRB2-Sos complex. Proline 48-55 growth factor receptor bound protein 2 Homo sapiens 128-132 8649768-2 1996 IsfI and IsfII nucleotide sequences differ only by the presence in IsfII of an inframe 45 hp insertion located near the first proline-rich motif required for Grb2 binding. Proline 126-133 growth factor receptor bound protein 2 Homo sapiens 158-162 7566970-7 1995 Inhibition studies with BIAcore using proline rich peptides derived from the C-terminus of Sos1 show that there is a single major binding site for Grb2 in Sos1. Proline 38-45 growth factor receptor bound protein 2 Homo sapiens 147-151 7592693-9 1995 Both Grb2 and EGF receptors are released from Cbl in the presence of a proline-rich peptide that binds the NH2-terminal SH3 domain of Grb2. Proline 71-78 growth factor receptor bound protein 2 Homo sapiens 134-138 7592693-10 1995 These results indicate that autophosphorylated EGF receptors associate with the SH2 domain of Grb2, which is complexed through its SH3 domain with proline-rich regions of Cbl. Proline 147-154 growth factor receptor bound protein 2 Homo sapiens 94-98 8585605-3 1995 In order to examine molecular determinants of the proline motif:SH3 interaction, an enzyme-linked immunosorbent assay was developed to observe binding of 5-lipoxygenase to SH3 domains of growth factor receptor binding protein 2 (Grb2). Proline 50-57 growth factor receptor bound protein 2 Homo sapiens 187-227 8585605-3 1995 In order to examine molecular determinants of the proline motif:SH3 interaction, an enzyme-linked immunosorbent assay was developed to observe binding of 5-lipoxygenase to SH3 domains of growth factor receptor binding protein 2 (Grb2). Proline 50-57 growth factor receptor bound protein 2 Homo sapiens 229-233 7642542-4 1995 This interaction is mediated by the SH3 domains of Grb2 and the proline-rich sequence PPPKIP in the carboxy-terminal region of SAP kinase. Proline 64-71 growth factor receptor bound protein 2 Homo sapiens 51-55 7629138-5 1995 We show that hSos2 interacts with Grb2 via its proline-rich COOH-terminal domain and that this interaction is dependent on the SH3 domains of Grb2. Proline 47-54 growth factor receptor bound protein 2 Homo sapiens 34-38 7752246-3 1995 Docking of the proline-rich peptide, 3BP1 on Grb2-N SH3, shows that the polyproline type II helix can bind the SH3 domain forming conserved hydrogen bonds between the main-chain carbonyl oxygens of Met4 and Pro7 of the proline-rich peptide and the reoriented side-chains of Trp36 and Asn51, respectively, and a hydrogen bond between the main-chain carbonyl of Leu8 of the proline rich peptide with the side-chain OH of Tyr52 of the Grb2-N SH3. Proline 15-22 growth factor receptor bound protein 2 Homo sapiens 432-436 7752246-3 1995 Docking of the proline-rich peptide, 3BP1 on Grb2-N SH3, shows that the polyproline type II helix can bind the SH3 domain forming conserved hydrogen bonds between the main-chain carbonyl oxygens of Met4 and Pro7 of the proline-rich peptide and the reoriented side-chains of Trp36 and Asn51, respectively, and a hydrogen bond between the main-chain carbonyl of Leu8 of the proline rich peptide with the side-chain OH of Tyr52 of the Grb2-N SH3. Proline 15-22 growth factor receptor bound protein 2 Homo sapiens 45-49 7752246-5 1995 The proline-rich peptides could bind the Grb2-N SH3 in either orientation and maintain the key hydrogen bonds because of the pseudo-symmetry of the polyproline type II helix. Proline 4-11 growth factor receptor bound protein 2 Homo sapiens 41-45 7773779-4 1994 1H NMR analysis of the complex between the Ser-32-GRB2-N-SH3 domain and the proline-rich peptide VPPPVPPRRR, derived from h-Sos, shows that relative to the SH3 peptide complexes described for PI3K, Fyn and Abl, the proline-rich peptide in this complex binds in the opposite orientation. Proline 76-83 growth factor receptor bound protein 2 Homo sapiens 50-54 7537212-4 1995 Both bind to the proline-rich C-terminal domain (PRD) of dynamin and inhibit the ability of microtubules and grb2 to stimulate GTPase activity. Proline 17-24 growth factor receptor bound protein 2 Homo sapiens 109-113 7773779-0 1994 NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos. Proline 74-81 growth factor receptor bound protein 2 Homo sapiens 46-50 7773779-2 1994 GRB2 couples receptor tyrosine kinase activation to Ras signalling by interacting, through its SH3 domains, to the carboxy-terminal proline-rich regions of the guanine nucleotide exchange factor Sos. Proline 132-139 growth factor receptor bound protein 2 Homo sapiens 0-4 7773779-4 1994 1H NMR analysis of the complex between the Ser-32-GRB2-N-SH3 domain and the proline-rich peptide VPPPVPPRRR, derived from h-Sos, shows that relative to the SH3 peptide complexes described for PI3K, Fyn and Abl, the proline-rich peptide in this complex binds in the opposite orientation. Proline 215-222 growth factor receptor bound protein 2 Homo sapiens 50-54 30282717-0 2019 The 11-Kilodalton Nonstructural Protein of Human Parvovirus B19 Facilitates Viral DNA Replication by Interacting with Grb2 through Its Proline-Rich Motifs. Proline 135-142 growth factor receptor bound protein 2 Homo sapiens 118-122 7929073-1 1994 A short, proline-rich region spanning residues 566-577 in human 5-lipoxygenase is a binding site for the Src homology 3 (SH3) domain of growth factor receptor-bound protein 2 (Grb2), an "adaptor" protein for tyrosine kinase-mediated cell signaling. Proline 9-16 growth factor receptor bound protein 2 Homo sapiens 136-174 7929073-1 1994 A short, proline-rich region spanning residues 566-577 in human 5-lipoxygenase is a binding site for the Src homology 3 (SH3) domain of growth factor receptor-bound protein 2 (Grb2), an "adaptor" protein for tyrosine kinase-mediated cell signaling. Proline 9-16 growth factor receptor bound protein 2 Homo sapiens 176-180 7929073-3 1994 A peptide corresponding to the proline-rich, SH3-binding motif inhibited formation of the 5-lipoxygenase.Grb2 complex in vitro. Proline 31-38 growth factor receptor bound protein 2 Homo sapiens 105-109 8402898-3 1993 Selective binding to a subset of 15 different recombinant SH3 domains occurs through proline-rich sequence motifs similar to those that mediate the interaction of the SH3 domains of Grb2 and Abl proteins to the guanine nucleotide exchange protein, Sos, and to the 3BP1 protein, respectively. Proline 85-92 growth factor receptor bound protein 2 Homo sapiens 182-186 30282717-6 2019 In vitro, one proline-rich motif was sufficient for 11-kDa to sustain a strong interaction with Grb2. Proline 14-21 growth factor receptor bound protein 2 Homo sapiens 96-100 30282717-15 2019 In vitro, 11-kDa interacts with Grb2 with high affinity through three proline-rich motifs, of which at least one is indispensable for the regulation of viral DNA replication. Proline 70-77 growth factor receptor bound protein 2 Homo sapiens 32-36 28455498-5 2017 The C-terminal SH3 domain (SH3C) of Grb2 bivalently interacts with the atypical non-PxxP proline rich region of SLP65, and the N-terminal SH3 domain (SH3N) of Vav, both the interactions crucial for the proper functioning of the B cell. Proline 89-96 growth factor receptor bound protein 2 Homo sapiens 36-40 22253690-5 2012 Adapter molecules such as Grb2 and CrkL interact with proline-rich region and activate multiple Bcr-Abl downstream signaling pathways that contribute to growth and survival. Proline 54-61 growth factor receptor bound protein 2 Homo sapiens 26-30 26286913-12 2015 SH3BGRL3 interacts with phosphor-EGFR at Y1068, Y1086, and Y1173 through Grb2 by its proline-rich motif, and activates the Akt-associated signaling pathway. Proline 85-92 growth factor receptor bound protein 2 Homo sapiens 73-77 24105423-0 2013 Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR. Proline 37-44 growth factor receptor bound protein 2 Homo sapiens 71-75 24105423-2 2013 The N-terminal SH3 (nSH3) domain of Grb2 binds a proline-rich region present in the guanine nucleotide releasing factor, son of sevenless (Sos). Proline 49-56 growth factor receptor bound protein 2 Homo sapiens 36-40 24105423-3 2013 Using NMR relaxation dispersion and chemical shift analysis methods, we investigated the conformational change of the Sos-derived proline-rich peptide during the transition between the free and Grb2 nSH3-bound states. Proline 130-137 growth factor receptor bound protein 2 Homo sapiens 194-198 24098653-7 2013 In all previously reported crystal structures, the peptide bound to the Grb2 SH2 domains adopts a type-I beta-turn conformation, except those with a proline residue at the pY+3 position. Proline 149-156 growth factor receptor bound protein 2 Homo sapiens 72-76 23460737-3 2013 In this article, we show that THEMIS and the adapter molecule growth factor receptor-bound protein 2 (GRB2) associate constitutively through binding of a conserved PxRPxK motif within the proline-rich region 1 of THEMIS to the C-terminal SH3-domain of GRB2. Proline 188-195 growth factor receptor bound protein 2 Homo sapiens 62-100 23460737-3 2013 In this article, we show that THEMIS and the adapter molecule growth factor receptor-bound protein 2 (GRB2) associate constitutively through binding of a conserved PxRPxK motif within the proline-rich region 1 of THEMIS to the C-terminal SH3-domain of GRB2. Proline 188-195 growth factor receptor bound protein 2 Homo sapiens 102-106 23460737-3 2013 In this article, we show that THEMIS and the adapter molecule growth factor receptor-bound protein 2 (GRB2) associate constitutively through binding of a conserved PxRPxK motif within the proline-rich region 1 of THEMIS to the C-terminal SH3-domain of GRB2. Proline 188-195 growth factor receptor bound protein 2 Homo sapiens 252-256 21508312-4 2011 Moreover, RhoU physically associates with activated EGFR in a GRB2-dependent manner through specific proline-rich motifs within its N-terminus. Proline 101-108 growth factor receptor bound protein 2 Homo sapiens 62-66 21745501-5 2011 The binding is mediated by the proline-rich sequence of Tat and the SH3 domain of Grb2. Proline 31-38 growth factor receptor bound protein 2 Homo sapiens 82-86 18789888-2 2008 Here, we show that Grb2, an SH3 domain-containing adaptor protein, binds to the proline-rich domain of FasL and regulates its cell surface expression. Proline 80-87 growth factor receptor bound protein 2 Homo sapiens 19-23 20643654-5 2010 A proline-rich sequence in PDK1 bound to an Src homology 3 domain in Grb2 in response to IGF-I. Proline 2-9 growth factor receptor bound protein 2 Homo sapiens 69-73 20643654-6 2010 Disruption of Grb2-PDK1 by expression of either a Grb2 Src homology 3 domain or a PDK1 proline to alanine mutant inhibited PDK1 recruitment to SHPS-1, leading to impaired IGF-I-stimulated AKT Thr(308) phosphorylation. Proline 87-94 growth factor receptor bound protein 2 Homo sapiens 14-18 20554525-7 2010 Furthermore, Grb2 did not bind to a single region but rather to different regions of NPM-ALK, mainly Tyr(152-156), Tyr(567), and a proline-rich region, Pro(415-417). Proline 131-138 growth factor receptor bound protein 2 Homo sapiens 13-17 20554525-7 2010 Furthermore, Grb2 did not bind to a single region but rather to different regions of NPM-ALK, mainly Tyr(152-156), Tyr(567), and a proline-rich region, Pro(415-417). Proline 152-155 growth factor receptor bound protein 2 Homo sapiens 13-17 19815557-4 2009 Unlike the interaction between MIG6 and EGFR, our data suggest that these receptor tyrosine kinases require the adaptor protein Grb2 for efficient binding, which interacts with highly conserved proline-rich regions that are conserved between ACK1 and MIG6. Proline 194-201 growth factor receptor bound protein 2 Homo sapiens 128-132 19509291-5 2009 Grb2 was identified as its binding partner, and the proline-rich motifs of GAREM are recognized by the N- and C-terminal SH3 domains of Grb2. Proline 52-59 growth factor receptor bound protein 2 Homo sapiens 0-4 19509291-5 2009 Grb2 was identified as its binding partner, and the proline-rich motifs of GAREM are recognized by the N- and C-terminal SH3 domains of Grb2. Proline 52-59 growth factor receptor bound protein 2 Homo sapiens 136-140 19109251-6 2009 Unlike previous reports for the EGF RTK, which requires the Eps15 ubiquitin interacting motif, recruitment of Eps15 to Met involves the coiled-coil domain of Eps15 and the signaling adaptor molecule, Grb2, which binds through a proline-rich motif in the third domain of Eps15. Proline 228-235 growth factor receptor bound protein 2 Homo sapiens 200-204 18778683-1 2008 Grb2-Sos1 interaction, mediated by the canonical binding of N-terminal SH3 (nSH3) and C-terminal SH3 (cSH3) domains of Grb2 to a proline-rich sequence in Sos1, provides a key regulatory switch that relays signaling from activated receptor tyrosine kinases to downstream effector molecules such as Ras. Proline 129-136 growth factor receptor bound protein 2 Homo sapiens 0-4 18778683-1 2008 Grb2-Sos1 interaction, mediated by the canonical binding of N-terminal SH3 (nSH3) and C-terminal SH3 (cSH3) domains of Grb2 to a proline-rich sequence in Sos1, provides a key regulatory switch that relays signaling from activated receptor tyrosine kinases to downstream effector molecules such as Ras. Proline 129-136 growth factor receptor bound protein 2 Homo sapiens 119-123 18620523-3 2008 RESULTS/CONCLUSION: Grb2 is a key molecule in intracellular signal transduction, linking activated cell surface receptors to downstream targets by binding to specific phosphotyrosine-containing and proline-rich sequence motifs. Proline 198-205 growth factor receptor bound protein 2 Homo sapiens 20-24 17113302-4 2007 We report the synthesis of new Grb2 ligands in which the key Val5 residue has been replaced by a cis C(beta)-substituted proline. Proline 121-128 growth factor receptor bound protein 2 Homo sapiens 31-35 17869481-4 2007 The N-SH3 domain of Grb2 is linked to a proline-rich sequence of the C2 domain of PLC-gamma1, PLC-gamma1 itself is linked, through its SH3 domain, to the C-terminal proline-rich region of Sos. Proline 40-47 growth factor receptor bound protein 2 Homo sapiens 20-24 17869481-4 2007 The N-SH3 domain of Grb2 is linked to a proline-rich sequence of the C2 domain of PLC-gamma1, PLC-gamma1 itself is linked, through its SH3 domain, to the C-terminal proline-rich region of Sos. Proline 165-172 growth factor receptor bound protein 2 Homo sapiens 20-24 16893902-3 2006 Spry2 is considerably more inhibitory than Spry1 or Spry4, and this correlates with the binding to Grb2 via a C-terminal proline-rich sequence that is found exclusively on Spry2. Proline 121-128 growth factor receptor bound protein 2 Homo sapiens 99-103 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Proline 186-193 growth factor receptor bound protein 2 Homo sapiens 232-236 16906159-4 2006 In T cells, the SH2 domain of GRB2 binds phosphorylated tyrosines on the adaptor protein LAT and the GRB2 SH3 domains associate with the proline-rich regions of SOS1 and CBL. Proline 137-144 growth factor receptor bound protein 2 Homo sapiens 30-34 16906159-4 2006 In T cells, the SH2 domain of GRB2 binds phosphorylated tyrosines on the adaptor protein LAT and the GRB2 SH3 domains associate with the proline-rich regions of SOS1 and CBL. Proline 137-144 growth factor receptor bound protein 2 Homo sapiens 101-105 16480678-5 2006 We subsequently describe a very rapid 96-well screening of inhibitors based on a simple competition between purified Grb2 and a peroxidase-coupled proline-rich peptide. Proline 147-154 growth factor receptor bound protein 2 Homo sapiens 117-121 16520382-4 2006 The NH(2)-terminal proline-rich collagen homology 2 (CH2) domain of p66shc associates with full-length grb2 in vitro via the COOH-terminal src homology 3 (C-SH3) domain of grb2. Proline 19-26 growth factor receptor bound protein 2 Homo sapiens 103-107 16520382-4 2006 The NH(2)-terminal proline-rich collagen homology 2 (CH2) domain of p66shc associates with full-length grb2 in vitro via the COOH-terminal src homology 3 (C-SH3) domain of grb2. Proline 19-26 growth factor receptor bound protein 2 Homo sapiens 172-176 16520382-6 2006 The CH2 domain competes with the proline-rich COOH-terminal region of sos1 for the C-SH3 domain of grb2. Proline 33-40 growth factor receptor bound protein 2 Homo sapiens 99-103 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Proline 186-193 growth factor receptor bound protein 2 Homo sapiens 269-273 15486046-12 2005 In summary, 1) SHIP-WT and SHIPDeltaIP expression inhibit insulin and PDGF stimulated Ras, MAPK kinase, and MAPK activities; 2) SHIP associates with tyrosine phosphorylated Shc, and the proline-rich sequences in SHIP associate with Grb2 and titrate out SOS to form Shc*Grb2*SHIP complexes; and 3) dissociation of SOS from the Shc*Grb2 complex inhibits Ras GTP loading, leading to decreased signaling through the MAPK pathway. Proline 186-193 growth factor receptor bound protein 2 Homo sapiens 269-273 14679214-7 2004 A proline-rich sequence of Son of Sevenless also specifically bound Grb2, demonstrating that the screen maintains specificity with low affinity interactions. Proline 2-9 growth factor receptor bound protein 2 Homo sapiens 68-72 12522133-6 2003 A cell-permeant TAT-tagged peptide encompassing the second proline-rich SH3 binding domain of PAK1 simultaneously blocked Grb2 and activated EGFR association with PAK1, in vitro and in vivo, indicating that Grb2 mediates the interaction of PAK1 with the activated EGFR. Proline 59-66 growth factor receptor bound protein 2 Homo sapiens 122-126 12839496-5 2003 Localization of Cbl-yellow fluorescent protein to these endocytic organelles was dependent on a proline-rich domain of c-Cbl that interacts with Grb2 as shown by fluorescence resonance energy transfer microscopy. Proline 96-103 growth factor receptor bound protein 2 Homo sapiens 145-149 12522133-6 2003 A cell-permeant TAT-tagged peptide encompassing the second proline-rich SH3 binding domain of PAK1 simultaneously blocked Grb2 and activated EGFR association with PAK1, in vitro and in vivo, indicating that Grb2 mediates the interaction of PAK1 with the activated EGFR. Proline 59-66 growth factor receptor bound protein 2 Homo sapiens 207-211 12399475-4 2002 Grb2 and RN-tre associate both in vitro and in vivo, with interaction mediated by both SH3 domains of Grb2 and extended proline-rich sequences in RN-tre. Proline 120-127 growth factor receptor bound protein 2 Homo sapiens 0-4 11964172-2 2002 In order to study the role of Grb2 in blood platelet responses, we used a peptide containing two proline-rich sequences derived from Sos (peptidimer), which binds to Grb2-Src homology 3 domain (SH3) with a high affinity, and hence inhibits Grb2-SH3-mediated protein interactions. Proline 97-104 growth factor receptor bound protein 2 Homo sapiens 166-170 11964172-2 2002 In order to study the role of Grb2 in blood platelet responses, we used a peptide containing two proline-rich sequences derived from Sos (peptidimer), which binds to Grb2-Src homology 3 domain (SH3) with a high affinity, and hence inhibits Grb2-SH3-mediated protein interactions. Proline 97-104 growth factor receptor bound protein 2 Homo sapiens 166-170 11964172-5 2002 Grb2-SH3 domains formed an association with the proline-rich sequences of Sos and Cbl in both resting and activated platelets, since the peptidimer abolished these associations. Proline 48-55 growth factor receptor bound protein 2 Homo sapiens 0-4 11878897-3 2001 Mutation of prolines within one of the three SH3 ligand-like sequences decreases the binding of B19 11-kDa proteins to Grb2, suggesting that the proline-rich region is involved in the B19 11-kDa/Grb2 interaction. Proline 12-20 growth factor receptor bound protein 2 Homo sapiens 119-123 11878897-3 2001 Mutation of prolines within one of the three SH3 ligand-like sequences decreases the binding of B19 11-kDa proteins to Grb2, suggesting that the proline-rich region is involved in the B19 11-kDa/Grb2 interaction. Proline 12-20 growth factor receptor bound protein 2 Homo sapiens 195-199 11878897-3 2001 Mutation of prolines within one of the three SH3 ligand-like sequences decreases the binding of B19 11-kDa proteins to Grb2, suggesting that the proline-rich region is involved in the B19 11-kDa/Grb2 interaction. Proline 12-19 growth factor receptor bound protein 2 Homo sapiens 119-123 11878897-3 2001 Mutation of prolines within one of the three SH3 ligand-like sequences decreases the binding of B19 11-kDa proteins to Grb2, suggesting that the proline-rich region is involved in the B19 11-kDa/Grb2 interaction. Proline 12-19 growth factor receptor bound protein 2 Homo sapiens 195-199 11726515-4 2001 Tyr209 within the C-terminal SH3 domain of Grb2 was identified as one of the tyrosine phosphorylation sites, and phosphorylation of Tyr209 abolished the binding of the SH3 domain to a proline-rich Sos peptide in vitro. Proline 184-191 growth factor receptor bound protein 2 Homo sapiens 43-47 11509578-5 2001 The new protein mainly binds to the proline-rich region of mDia through its Src homology 3 domain and also binds to Grb2 through its proline-rich domain. Proline 36-43 growth factor receptor bound protein 2 Homo sapiens 116-120 11509578-5 2001 The new protein mainly binds to the proline-rich region of mDia through its Src homology 3 domain and also binds to Grb2 through its proline-rich domain. Proline 133-140 growth factor receptor bound protein 2 Homo sapiens 116-120 11353842-4 2001 Furthermore, Grb2 bound to tyrosine-phosphorylated FRS2 through its SH2 domain interacts primarily via its carboxyl-terminal SH3 domain with a proline-rich region in Gab1 and via its amino-terminal SH3 domain with the nucleotide exchange factor Sos1. Proline 143-150 growth factor receptor bound protein 2 Homo sapiens 13-17 11533253-13 2001 We conclude that proline-rich motifs within the N terminus of PI3K-C2beta mediate the association of this enzyme with activated EGF receptor and that this interaction involves the Grb2 adaptor. Proline 17-24 growth factor receptor bound protein 2 Homo sapiens 180-184 11371563-6 2001 Using sequence-specific peptides, we found that the second proline-rich domain of DOC-2/DAB2 is the key binding site to Grb2 in the presence of growth factors. Proline 59-66 growth factor receptor bound protein 2 Homo sapiens 120-124 11178911-6 2001 Binding experiments on Grb2 and peptides containing two different proline-rich sequences indicate that Grb2 adapts the relative position and orientation of the two SH3 domains to bind bivalently to the target peptide sequences. Proline 66-73 growth factor receptor bound protein 2 Homo sapiens 23-27 11278754-3 2001 The interaction requires the C-terminal SH3-domain of Grb2/3-3 and the proline-rich sequence contained in p27 immediately downstream of the Cdk binding domain. Proline 71-78 growth factor receptor bound protein 2 Homo sapiens 54-58 11178911-6 2001 Binding experiments on Grb2 and peptides containing two different proline-rich sequences indicate that Grb2 adapts the relative position and orientation of the two SH3 domains to bind bivalently to the target peptide sequences. Proline 66-73 growth factor receptor bound protein 2 Homo sapiens 103-107 11746524-2 2001 The SH2 domain of Grb2 recognizes and interacts with phosphotyrosine residues on activated tyrosine kinases, whereas the SH3 domains bind to several proline-rich domain-containing proteins such as Sos1. Proline 149-156 growth factor receptor bound protein 2 Homo sapiens 18-22