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• W2164865257 endingPage "8077" @default.
• W2164865257 startingPage "8072" @default.
• W2164865257 abstract "The GGAs (Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding proteins) are a family of proteins implicated in protein trafficking from the Golgi to endosomes/lysosomes. These proteins have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (gamma-adaptin ear) domain. Isolated VHS domains have been shown to bind specifically to acidic cluster (AC)-dileucine motifs present in the cytoplasmic tails of the mannose 6-phosphate receptors. Here we report that full-length cytoplasmic GGA1 and GGA3 but not GGA2 bind the cation-independent mannose 6-phosphate receptor very poorly because of autoinhibition. This inhibition is caused by the binding of an AC-LL sequence present in the hinge segment to the ligand-binding site in the VHS domain. The inhibition depends on the phosphorylation of a serine located three residues upstream of the AC-LL motif. The serine is phosphorylated by casein kinase 2 in in vitro assays. Substitution of the GGA1 inhibitory sequence into the analogous location in GGA2, which lacks the AC-LL motif, results in autoinhibition of the latter protein. These data indicate that the activity of GGA1 and GGA3 is regulated by cycles of phosphorylation/dephosphorylation." @default.
• W2164865257 created "2016-06-24" @default.
• W2164865257 creator A5013498569 @default.
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• W2164865257 creator A5041296489 @default.
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• W2164865257 date "2002-06-11" @default.
• W2164865257 modified "2023-10-14" @default.
• W2164865257 title "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif" @default.
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• W2164865257 doi "https://doi.org/10.1073/pnas.082235699" @default.
• W2164865257 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/123022" @default.
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