{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Goto A"],"funding":["Japan Agency for Medical Research and Development","Japan Society for the Promotion of Science"],"pagination":["8576"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9368931"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(15)"],"pubmed_abstract":["Ceramide transport protein (CERT) mediates ceramide transfer from the endoplasmic reticulum to the Golgi for sphingomyelin (SM) biosynthesis. CERT is inactivated by multiple phosphorylation at the serine-repeat motif (SRM), and mutations that impair the SRM phosphorylation are associated with a group of inherited intellectual disorders in humans. It has been suggested that the <i>N</i>-terminal phosphatidylinositol 4-monophosphate [PtdIns(4)P] binding domain and the <i>C</i>-terminal ceramide-transfer domain of CERT physically interfere with each other in the SRM phosphorylated state, thereby repressing the function of CERT; however, it remains unclear which regions in CERT are involved in the SRM phosphorylation-dependent repression of CERT. Here, we identified a previously uncharacterize"],"journal":["International journal of molecular sciences"],"pubmed_title":["Involvement of a Cluster of Basic Amino Acids in Phosphorylation-Dependent Functional Repression of the Ceramide Transport Protein CERT."],"pmcid":["PMC9368931"],"funding_grant_id":["JP20gm0910005j0006","18K06649"],"pubmed_authors":["Kumagai K","Egawa D","Yamaji T","Tomishige N","Goto A","Shimasaki K","Hanada K"],"additional_accession":[]},"is_claimable":false,"name":"Involvement of a Cluster of Basic Amino Acids in Phosphorylation-Dependent Functional Repression of the Ceramide Transport Protein CERT.","description":"Ceramide transport protein (CERT) mediates ceramide transfer from the endoplasmic reticulum to the Golgi for sphingomyelin (SM) biosynthesis. CERT is inactivated by multiple phosphorylation at the serine-repeat motif (SRM), and mutations that impair the SRM phosphorylation are associated with a group of inherited intellectual disorders in humans. It has been suggested that the <i>N</i>-terminal phosphatidylinositol 4-monophosphate [PtdIns(4)P] binding domain and the <i>C</i>-terminal ceramide-transfer domain of CERT physically interfere with each other in the SRM phosphorylated state, thereby repressing the function of CERT; however, it remains unclear which regions in CERT are involved in the SRM phosphorylation-dependent repression of CERT. Here, we identified a previously uncharacterize","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2025-04-04T10:44:52.347Z","creation":"2025-02-19T01:55:43.923Z"},"accession":"S-EPMC9368931","cross_references":{"pubmed":["35955719"],"doi":["10.3390/ijms23158576"]}}