{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Roncagalli R"],"funding":["European Research Council","Agence Nationale de la Recherche","Institut National de la Santé et de la Recherche Médicale","Centre National de la Recherche Scientifique","Axa Research Fund"],"pagination":["2437-2457"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5068240"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["213(11)"],"pubmed_abstract":["The RLTPR cytosolic protein, also known as CARMIL2, is essential for CD28 co-stimulation in mice, but its importance in human T cells and mode of action remain elusive. Here, using affinity purification followed by mass spectrometry analysis, we showed that RLTPR acts as a scaffold, bridging CD28 to the CARD11/CARMA1 cytosolic adaptor and to the NF-κB signaling pathway, and identified proteins not found before within the CD28 signaling pathway. We further demonstrated that RLTPR is essential for CD28 co-stimulation in human T cells and that its noncanonical pleckstrin-homology domain, leucine-rich repeat domain, and proline-rich region were mandatory for that task. Although RLTPR is thought to function as an actin-uncapping protein, this property was dispensable for CD28 co-stimulation in "],"journal":["The Journal of experimental medicine"],"pubmed_title":["The scaffolding function of the RLTPR protein explains its essential role for CD28 co-stimulation in mouse and human T cells."],"pmcid":["PMC5068240"],"funding_grant_id":["322465"],"pubmed_authors":["Jarmuzynski N","Roncagalli R","Liang Y","Joachim A","Bergot E","Camoin L","Gregoire C","Zhang L","Malissen B","Suchanek M","Durand S","Malissen M","Cucchetti M","Fiore F","Baudelet E","Audebert S","Menoita MG"],"additional_accession":[]},"is_claimable":false,"name":"The scaffolding function of the RLTPR protein explains its essential role for CD28 co-stimulation in mouse and human T cells.","description":"The RLTPR cytosolic protein, also known as CARMIL2, is essential for CD28 co-stimulation in mice, but its importance in human T cells and mode of action remain elusive. Here, using affinity purification followed by mass spectrometry analysis, we showed that RLTPR acts as a scaffold, bridging CD28 to the CARD11/CARMA1 cytosolic adaptor and to the NF-κB signaling pathway, and identified proteins not found before within the CD28 signaling pathway. We further demonstrated that RLTPR is essential for CD28 co-stimulation in human T cells and that its noncanonical pleckstrin-homology domain, leucine-rich repeat domain, and proline-rich region were mandatory for that task. Although RLTPR is thought to function as an actin-uncapping protein, this property was dispensable for CD28 co-stimulation in ","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Oct","modification":"2026-04-30T01:10:16.219Z","creation":"2019-03-27T02:26:57Z"},"accession":"S-EPMC5068240","cross_references":{"pubmed":["27647348"],"doi":["10.1084/jem.20160579"]}}