{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Garcia-Ortiz A"],"funding":["European Research Council"],"pagination":["e2000653"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5386235"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(4)"],"pubmed_abstract":["The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-θ (PKC-θ) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of β-actin and PKC-θ from the lamellipodium-like distal (d)-SMAC, promoting PKC-θ activation. Furthermore, eNOS-derived NO S-nitrosylated β-actin on Cys374 and impaired actin binding to profilin-1 (PFN1), as confirmed with the transnitrosyla"],"journal":["PLoS biology"],"pubmed_title":["eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1."],"pmcid":["PMC5386235"],"funding_grant_id":["294340"],"pubmed_authors":["Martinez-Ruiz A","Ibiza S","Vazquez J","Trullo A","Sanchez-Madrid F","Victor VM","Garcia-Ortiz A","Ortega A","Izquierdo-Alvarez A","Serrador JM","Calvo E","Martin-Cofreces NB","Sot B"],"additional_accession":[]},"is_claimable":false,"name":"eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.","description":"The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-θ (PKC-θ) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of β-actin and PKC-θ from the lamellipodium-like distal (d)-SMAC, promoting PKC-θ activation. Furthermore, eNOS-derived NO S-nitrosylated β-actin on Cys374 and impaired actin binding to profilin-1 (PFN1), as confirmed with the transnitrosyla","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Apr","modification":"2026-04-08T17:12:15.875Z","creation":"2019-03-26T22:46:18Z"},"accession":"S-EPMC5386235","cross_references":{"pubmed":["28394935"],"doi":["10.1371/journal.pbio.2000653"]}}