<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>10(10)</volume><submitter>Buchse T</submitter><pubmed_abstract>The Cbl-interacting 85-kDa protein (CIN85) plays an important role as a negative regulator of signaling pathways induced by receptor tyrosine kinases. By assembling multiprotein complexes this versatile adaptor enhances receptor tyrosine kinase-activated clathrin-mediated endocytosis and reduces phosphatidylinositol-3-kinase-induced phosphatidylinositol-3,4,5-trisphosphate production. Here we report the expression of CIN85 in primary splenic B lymphocytes and the B-lymphoma cell lines WEHI 231 and Ba/F3. Cross-linking of the B cell antigen receptor resulted in an increased association of CIN85 with the ubiquitin ligase Cbl. Through a systematic pull-down proteomics approach we identified 51 proteins that interact with CIN85 in B cells, including proteins not shown previously to be CIN85-as</pubmed_abstract><journal>Molecular &amp; cellular proteomics : MCP</journal><pagination>M110.006239</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3205855</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>CIN85 interacting proteins in B cells-specific role for SHIP-1.</pubmed_title><pmcid>PMC3205855</pmcid><pubmed_authors>Horras N</pubmed_authors><pubmed_authors>Mikkat S</pubmed_authors><pubmed_authors>Lenfert E</pubmed_authors><pubmed_authors>Tiedge M</pubmed_authors><pubmed_authors>Korbel S</pubmed_authors><pubmed_authors>Krystal G</pubmed_authors><pubmed_authors>Krause E</pubmed_authors><pubmed_authors>Schumann M</pubmed_authors><pubmed_authors>Buchse T</pubmed_authors></additional><is_claimable>false</is_claimable><name>CIN85 interacting proteins in B cells-specific role for SHIP-1.</name><description>The Cbl-interacting 85-kDa protein (CIN85) plays an important role as a negative regulator of signaling pathways induced by receptor tyrosine kinases. By assembling multiprotein complexes this versatile adaptor enhances receptor tyrosine kinase-activated clathrin-mediated endocytosis and reduces phosphatidylinositol-3-kinase-induced phosphatidylinositol-3,4,5-trisphosphate production. Here we report the expression of CIN85 in primary splenic B lymphocytes and the B-lymphoma cell lines WEHI 231 and Ba/F3. Cross-linking of the B cell antigen receptor resulted in an increased association of CIN85 with the ubiquitin ligase Cbl. Through a systematic pull-down proteomics approach we identified 51 proteins that interact with CIN85 in B cells, including proteins not shown previously to be CIN85-as</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Oct</publication><modification>2025-04-18T17:24:56.302Z</modification><creation>2019-06-05T16:51:31Z</creation></dates><accession>S-EPMC3205855</accession><cross_references><pubmed>21725061</pubmed><doi>10.1074/mcp.m110.006239</doi><doi>10.1074/mcp.M110.006239</doi></cross_references></HashMap>