<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>162(4)</volume><submitter>Vindis C</submitter><pubmed_abstract>Eph receptors and their ligands (ephrins) play an important role in axonal guidance, topographic mapping, and angiogenesis. The signaling pathways mediating these activities are starting to emerge and are highly cell- and receptor-type specific. Here we demonstrate that activated EphB1 recruits the adaptor proteins Grb2 and p52Shc and promotes p52Shc and c-Src tyrosine phosphorylation as well as MAPK/extracellular signal-regulated kinase (ERK) activation. EphB1-mediated increase of cell migration was abrogated by the MEK inhibitor PD98059 and Src inhibitor PP2. In contrast, cell adhesion, which we previously showed to be c-jun NH2-terminal kinase (JNK) dependent, was unaffected by ERK1/2 and Src inhibition. Expression of dominant-negative c-Src significantly reduced EphB1-dependent ERK1/2 </pubmed_abstract><journal>The Journal of cell biology</journal><pagination>661-71</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2173797</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis.</pubmed_title><pmcid>PMC2173797</pmcid><pubmed_authors>Daniel TO</pubmed_authors><pubmed_authors>Cerretti DP</pubmed_authors><pubmed_authors>Huynh-Do U</pubmed_authors><pubmed_authors>Vindis C</pubmed_authors></additional><is_claimable>false</is_claimable><name>EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis.</name><description>Eph receptors and their ligands (ephrins) play an important role in axonal guidance, topographic mapping, and angiogenesis. The signaling pathways mediating these activities are starting to emerge and are highly cell- and receptor-type specific. Here we demonstrate that activated EphB1 recruits the adaptor proteins Grb2 and p52Shc and promotes p52Shc and c-Src tyrosine phosphorylation as well as MAPK/extracellular signal-regulated kinase (ERK) activation. EphB1-mediated increase of cell migration was abrogated by the MEK inhibitor PD98059 and Src inhibitor PP2. In contrast, cell adhesion, which we previously showed to be c-jun NH2-terminal kinase (JNK) dependent, was unaffected by ERK1/2 and Src inhibition. Expression of dominant-negative c-Src significantly reduced EphB1-dependent ERK1/2 </description><dates><release>2003-01-01T00:00:00Z</release><publication>2003 Aug</publication><modification>2025-04-18T15:22:13.815Z</modification><creation>2019-03-26T23:01:25Z</creation></dates><accession>S-EPMC2173797</accession><cross_references><pubmed>12925710</pubmed><doi>10.1083/jcb.200302073</doi></cross_references></HashMap>