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• W2104097023 abstract "The R-SNARE VAMP4, which contains a dileucine motif, binds to the AP-1 (adaptor protein-1) subunit mu 1a, but not mu 1b, or the GGAs (Golgi-associated gamma ear containing ARF binding proteins). Serine 20 and leucines 25,26 are essential for this binding. AP-1 association with VAMP4 is enhanced when serine 30, in an acidic cluster, is phosphorylated by casein kinase 2. This phosphorylation-dependent modulation of AP-1 binding is mediated by PACS-1 (phosphofurin acidic cluster sorting protein). Ablation of both the dileucine motif and serine 30 results in a dramatic mislocalization of VAMP4 in the regulated secretory pathway in AtT20 cells. A dominant-negative PACS-1, which binds acidic clusters but not AP-1, also causes mislocalization of VAMP4. Our data support a model whereby phosphorylation-dependent recruitment of PACS-1 enhances AP-1 association to cargo, and suggest that efficient retrieval depends on the formation of a complex between cargo, such as VAMP4, AP-1 and PACS-1." @default.
• W2104097023 created "2016-06-24" @default.
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• W2104097023 date "2003-12-01" @default.
• W2104097023 modified "2023-10-14" @default.
• W2104097023 title "AP‐1 recruitment to VAMP4 is modulated by phosphorylation‐dependent binding of PACS‐1" @default.
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• W2104097023 doi "https://doi.org/10.1038/sj.embor.7400018" @default.
• W2104097023 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1326413" @default.
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