<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Rios KE</submitter><funding>National Institute of Allergy and Infectious Diseases</funding><funding>NIAID NIH HHS</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>104179</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7484395</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>356</volume><pubmed_abstract>After T cell receptor (TCR) engagement, the CARD11-Bcl10-Malt1 (CBM) complex oligomerizes to transduce NF-κB activating signals. Bcl10 is then degraded to limit NF-κB activation. The cDNA AK057716 (BinCARD-1) was reported to encode a novel CARD protein that interacts with Bcl10 and modestly inhibits NF-κB activation. In a later study, a second isoform, BinCARD-2, was identified. Here, we report that the cDNA AK057716 (BinCARD-1) is an incompletely spliced derivative of the gene product of C9orf89, whereas CARD19 (BinCARD-2) represents the properly spliced isoform, with conservation across diverse species. Immunoblotting revealed expression of CARD19 in T cells, but no evidence of BinCARD-1 expression, and microscopy demonstrated that endogenous CARD19 localizes to mitochondria. Although we</pubmed_abstract><journal>Cellular immunology</journal><pubmed_title>CARD19, the protein formerly known as BinCARD, is a mitochondrial protein that does not regulate Bcl10-dependent NF-κB activation after TCR engagement.</pubmed_title><pmcid>PMC7484395</pmcid><funding_grant_id>U01 GM109887</funding_grant_id><funding_grant_id>R01 AI125552</funding_grant_id><pubmed_authors>Rios KE</pubmed_authors><pubmed_authors>Maynard SK</pubmed_authors><pubmed_authors>Washington M</pubmed_authors><pubmed_authors>Schaefer BC</pubmed_authors><pubmed_authors>Paul S</pubmed_authors><pubmed_authors>Kashyap AK</pubmed_authors></additional><is_claimable>false</is_claimable><name>CARD19, the protein formerly known as BinCARD, is a mitochondrial protein that does not regulate Bcl10-dependent NF-κB activation after TCR engagement.</name><description>After T cell receptor (TCR) engagement, the CARD11-Bcl10-Malt1 (CBM) complex oligomerizes to transduce NF-κB activating signals. Bcl10 is then degraded to limit NF-κB activation. The cDNA AK057716 (BinCARD-1) was reported to encode a novel CARD protein that interacts with Bcl10 and modestly inhibits NF-κB activation. In a later study, a second isoform, BinCARD-2, was identified. Here, we report that the cDNA AK057716 (BinCARD-1) is an incompletely spliced derivative of the gene product of C9orf89, whereas CARD19 (BinCARD-2) represents the properly spliced isoform, with conservation across diverse species. Immunoblotting revealed expression of CARD19 in T cells, but no evidence of BinCARD-1 expression, and microscopy demonstrated that endogenous CARD19 localizes to mitochondria. Although we</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Oct</publication><modification>2026-05-07T19:36:06.801Z</modification><creation>2022-02-11T11:41:25.268Z</creation></dates><accession>S-EPMC7484395</accession><cross_references><pubmed>32763502</pubmed><doi>10.1016/j.cellimm.2020.104179</doi></cross_references></HashMap>