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| http://purl.uniprot.org/citations/15944398 | http://www.w3.org/2000/01/rdf-schema#comment | "Rho GTPases are important regulators for cell dynamics. They are activated by guanine nucleotide exchange factors and inactivated by GTPase-activating proteins (GAPs). We recently identified a novel RhoGAP, BPGAP1, that uses the BNIP-2 and Cdc42GAP homology (BCH) domain, RhoGAP domain and proline-rich region to regulate cell morphology and migration. To further explore its roles in intracellular signaling, we employed protein precipitations and matrix-assisted laser desorption/ionization mass-spectrometry and identified EEN/endophilin II as a novel partner of BPGAP1. EEN is a member of the endocytic endophilin family but its function in regulating endocytosis remains unclear. Pull-down and co-immunoprecipitation studies with deletion mutants confirmed that EEN interacted directly with BPGAP1 via its Src homology 3 (SH3) domain binding to the proline-rich region 182-PPPRPPLP-189 of BPGAP1, with prolines 184 and 186 being indispensable for this interaction. Overexpression of EEN or BPGAP1 alone induced EGF-stimulated receptor endocytosis and ERK1/2 phosphorylation. These processes were further enhanced when EEN was present together with the wildtype but not with the non-interactive proline mutant of BPGAP1. However, EEN lacking the SH3 domain served as a dominant negative mutant that completely inhibited these effects. Furthermore, BPGAP1 with a catalytically inactive GAP domain also blocked the effect of EEN and/or BPGAP1 in EGF receptor endocytosis and concomitantly reduced their level of augmentation for ERK1/2 phosphorylation. Our findings reveal a concomitant activation of endocytosis and ERK signaling by BPGAP1 via the coupling of its proline-rich region, which targets EEN and its functional GAP domain. BPGAP1 could therefore provide an important link between cytoskeletal network, endocytic trafficking and Ras/MAPK signaling."xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.02383"xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/author | "Low B.C."xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/author | "Lua B.L."xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/pages | "2707-2721"xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/title | "Activation of EGF receptor endocytosis and ERK1/2 signaling by BPGAP1 requires direct interaction with EEN/endophilin II and a functional RhoGAP domain."xsd:string |
| http://purl.uniprot.org/citations/15944398 | http://purl.uniprot.org/core/volume | "118"xsd:string |
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