{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ende RJ"],"funding":["National Institute of Allergy and Infectious Diseases"],"pagination":["e74535"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9286742"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["Membrane contact sites (MCS) are crucial for nonvesicular trafficking-based interorganelle communication. Endoplasmic reticulum (ER)-organelle tethering occurs in part through the interaction of the ER resident protein VAP with FFAT motif-containing proteins. FFAT motifs are characterized by a seven amino acidic core surrounded by acid tracks. We have previously shown that the human intracellular bacterial pathogen <i>Chlamydia trachomatis</i> establishes MCS between its vacuole (the inclusion) and the ER through expression of a bacterial tether, IncV, displaying molecular mimicry of eukaryotic FFAT motif cores. Here, we show that multiple layers of host cell kinase-mediated phosphorylation events govern the assembly of the IncV-VAP tethering complex and the formation of ER-Inclusion MCS. "],"journal":["eLife"],"pubmed_title":["Phosphoregulation accommodates Type III secretion and assembly of a tether of ER-<i>Chlamydia</i> inclusion membrane contact sites."],"pmcid":["PMC9286742"],"funding_grant_id":["AI162758","AI007046","AI136283","AI141841","AI101441","AI060767","AI166237"],"pubmed_authors":["Coppens I","Derre I","Murray RL","D'Spain SK","Ende RJ"],"additional_accession":[]},"is_claimable":false,"name":"Phosphoregulation accommodates Type III secretion and assembly of a tether of ER-<i>Chlamydia</i> inclusion membrane contact sites.","description":"Membrane contact sites (MCS) are crucial for nonvesicular trafficking-based interorganelle communication. Endoplasmic reticulum (ER)-organelle tethering occurs in part through the interaction of the ER resident protein VAP with FFAT motif-containing proteins. FFAT motifs are characterized by a seven amino acidic core surrounded by acid tracks. We have previously shown that the human intracellular bacterial pathogen <i>Chlamydia trachomatis</i> establishes MCS between its vacuole (the inclusion) and the ER through expression of a bacterial tether, IncV, displaying molecular mimicry of eukaryotic FFAT motif cores. Here, we show that multiple layers of host cell kinase-mediated phosphorylation events govern the assembly of the IncV-VAP tethering complex and the formation of ER-Inclusion MCS. ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2025-04-04T07:11:00.179Z","creation":"2025-02-19T03:22:14.144Z"},"accession":"S-EPMC9286742","cross_references":{"pubmed":["35838228"],"doi":["10.7554/eLife.74535"]}}