<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Serfass JM</submitter><funding>NHLBI NIH HHS</funding><funding>NCI NIH HHS</funding><funding>National Institutes of Health</funding><pagination>10097-10111</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5473216</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>292(24)</volume><pubmed_abstract>Endocytosis, and the subsequent trafficking of endosomes, requires dynamic physical alterations in membrane shape that are mediated in part by endophilin proteins. The endophilin B family of proteins contains an N-terminal Bin/amphiphysin/Rvs (N-BAR) domain that induces membrane curvature to regulate intracellular membrane dynamics. Whereas endophilin B1 (SH3GLB1/Bif-1) is known to be involved in a number of cellular processes, including apoptosis, autophagy, and endocytosis, the cellular function of endophilin B2 (SH3GLB2) is not well understood. In this study, we used genetic approaches that revealed that endophilin B2 is not required for embryonic development &lt;i>in vivo&lt;/i> but that endophilin B2 deficiency impairs endosomal trafficking &lt;i>in vitro&lt;/i>, as evidenced by suppressed endoso</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>Endophilin B2 facilitates endosome maturation in response to growth factor stimulation, autophagy induction, and influenza A virus infection.</pubmed_title><pmcid>PMC5473216</pmcid><funding_grant_id>HL128746</funding_grant_id><funding_grant_id>R56 HL128746</funding_grant_id><funding_grant_id>R01 CA129682</funding_grant_id><funding_grant_id>CA129682</funding_grant_id><funding_grant_id>R01 CA082197</funding_grant_id><funding_grant_id>CA82197</funding_grant_id><pubmed_authors>Liu Y</pubmed_authors><pubmed_authors>Tang Z</pubmed_authors><pubmed_authors>Yang L</pubmed_authors><pubmed_authors>Serfass JM</pubmed_authors><pubmed_authors>Young MM</pubmed_authors><pubmed_authors>Chroneos ZC</pubmed_authors><pubmed_authors>Atkinson JM</pubmed_authors><pubmed_authors>Kawasawa YI</pubmed_authors><pubmed_authors>Tsotakos N</pubmed_authors><pubmed_authors>Wang HG</pubmed_authors><pubmed_authors>Takahashi Y</pubmed_authors><pubmed_authors>Zhou Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Endophilin B2 facilitates endosome maturation in response to growth factor stimulation, autophagy induction, and influenza A virus infection.</name><description>Endocytosis, and the subsequent trafficking of endosomes, requires dynamic physical alterations in membrane shape that are mediated in part by endophilin proteins. The endophilin B family of proteins contains an N-terminal Bin/amphiphysin/Rvs (N-BAR) domain that induces membrane curvature to regulate intracellular membrane dynamics. Whereas endophilin B1 (SH3GLB1/Bif-1) is known to be involved in a number of cellular processes, including apoptosis, autophagy, and endocytosis, the cellular function of endophilin B2 (SH3GLB2) is not well understood. In this study, we used genetic approaches that revealed that endophilin B2 is not required for embryonic development &lt;i>in vivo&lt;/i> but that endophilin B2 deficiency impairs endosomal trafficking &lt;i>in vitro&lt;/i>, as evidenced by suppressed endoso</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jun</publication><modification>2025-04-05T11:59:10.847Z</modification><creation>2019-03-26T23:41:33Z</creation></dates><accession>S-EPMC5473216</accession><cross_references><pubmed>28455444</pubmed><doi>10.1074/jbc.m117.792747</doi><doi>10.1074/jbc.M117.792747</doi></cross_references></HashMap>