<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kao H</submitter><funding>NIAID NIH HHS</funding><pagination>8248-57</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2857686</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>181(12)</volume><pubmed_abstract>The mechanism underlying the transient accumulation of CD4 at the immunological synapse (IS) and its significance for T cell activation are not understood. To investigate these issues, we mutated a serine phosphorylation site (S408) in the cytoplasmic tail of murine CD4. Preventing phosphorylation of S408 did not block CD4 recruitment to the IS; rather, it blocked the ability of CD4 to leave the IS. Surprisingly, enhanced and prolonged CD4 accumulation at the supramolecular activation cluster in the contact area had no functional consequence for T cell activation, cytokine production, or proliferation. Protein kinase C theta (PKCtheta)-deficient T cells also displayed enhanced and prolonged accumulation of wild-type CD4 at the IS, indicating that theta is the critical PKC isoform involved </pubmed_abstract><journal>Journal of immunology (Baltimore, Md. : 1950)</journal><pubmed_title>Regulated movement of CD4 in and out of the immunological synapse.</pubmed_title><pmcid>PMC2857686</pmcid><funding_grant_id>P01 AI071195</funding_grant_id><funding_grant_id>AI071195</funding_grant_id><funding_grant_id>R37 AI024157</funding_grant_id><funding_grant_id>R37 AI024157-21</funding_grant_id><funding_grant_id>P01 AI071195-03</funding_grant_id><funding_grant_id>AI24157</funding_grant_id><funding_grant_id>R01 AI024157</funding_grant_id><pubmed_authors>Littman DR</pubmed_authors><pubmed_authors>Allen PM</pubmed_authors><pubmed_authors>Lin J</pubmed_authors><pubmed_authors>Shaw AS</pubmed_authors><pubmed_authors>Kao H</pubmed_authors></additional><is_claimable>false</is_claimable><name>Regulated movement of CD4 in and out of the immunological synapse.</name><description>The mechanism underlying the transient accumulation of CD4 at the immunological synapse (IS) and its significance for T cell activation are not understood. To investigate these issues, we mutated a serine phosphorylation site (S408) in the cytoplasmic tail of murine CD4. Preventing phosphorylation of S408 did not block CD4 recruitment to the IS; rather, it blocked the ability of CD4 to leave the IS. Surprisingly, enhanced and prolonged CD4 accumulation at the supramolecular activation cluster in the contact area had no functional consequence for T cell activation, cytokine production, or proliferation. Protein kinase C theta (PKCtheta)-deficient T cells also displayed enhanced and prolonged accumulation of wild-type CD4 at the IS, indicating that theta is the critical PKC isoform involved </description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Dec</publication><modification>2025-04-04T13:38:35.201Z</modification><creation>2019-03-26T23:42:52Z</creation></dates><accession>S-EPMC2857686</accession><cross_references><pubmed>19050241</pubmed><doi>10.4049/jimmunol.181.12.8248</doi></cross_references></HashMap>