{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lee S"],"funding":["NHLBI NIH HHS","NCI NIH HHS","NIH","NIGMS NIH HHS"],"pagination":["977-992"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6400557"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["218(3)"],"pubmed_abstract":["Regulation of plasma membrane (PM) protein abundance by selective endocytosis is critical for cellular adaptation to stress or changing nutrient availability. One example involves rapid endocytic turnover of Mup1, a yeast methionine transporter, in response to increased methionine availability. Here, we report that methionine triggers rapid translocation of the ubiquitin ligase adaptor Art1 to the PM and dephosphorylation of Art1 at specific threonine residues. This methionine-induced dephosphorylation of Art1 is mediated by Ppz phosphatases, and analysis of phosphomimetic and phosphorylation-defective variants of Art1 indicates that these events toggle Art1 recognition of Mup1 at the PM. Importantly, we find that Ppz phosphatases are dispensable for Art1 PM translocation, but are required"],"journal":["The Journal of cell biology"],"pubmed_title":["Methionine triggers Ppz-mediated dephosphorylation of Art1 to promote cargo-specific endocytosis."],"pmcid":["PMC6400557"],"funding_grant_id":["T32 CA119925","R01 GM118491","R00 GM101077","T32 HL069765"],"pubmed_authors":["Lee S","Ho HC","MacGurn JA","Tumolo JM","Hsu PC"],"additional_accession":[]},"is_claimable":false,"name":"Methionine triggers Ppz-mediated dephosphorylation of Art1 to promote cargo-specific endocytosis.","description":"Regulation of plasma membrane (PM) protein abundance by selective endocytosis is critical for cellular adaptation to stress or changing nutrient availability. One example involves rapid endocytic turnover of Mup1, a yeast methionine transporter, in response to increased methionine availability. Here, we report that methionine triggers rapid translocation of the ubiquitin ligase adaptor Art1 to the PM and dephosphorylation of Art1 at specific threonine residues. This methionine-induced dephosphorylation of Art1 is mediated by Ppz phosphatases, and analysis of phosphomimetic and phosphorylation-defective variants of Art1 indicates that these events toggle Art1 recognition of Mup1 at the PM. Importantly, we find that Ppz phosphatases are dispensable for Art1 PM translocation, but are required","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Mar","modification":"2026-06-04T00:58:43.875Z","creation":"2026-05-04T03:13:50.997Z"},"accession":"S-EPMC6400557","cross_references":{"pubmed":["30610170"],"doi":["10.1083/jcb.201712144"]}}