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- W2022169605 abstract "The trafficking of ion channels to the plasma membrane is tightly controlled to ensure the proper regulation of intracellular ion homeostasis and signal transduction. Mutations of polycystin-2, a member of the TRP family of cation channels, cause autosomal dominant polycystic kidney disease, a disorder characterized by renal cysts and progressive renal failure. Polycystin-2 functions as a calcium-permeable nonselective cation channel; however, it is disputed whether polycystin-2 resides and acts at the plasma membrane or endoplasmic reticulum (ER). We show that the subcellular localization and function of polycystin-2 are directed by phosphofurin acidic cluster sorting protein (PACS)-1 and PACS-2, two adaptor proteins that recognize an acidic cluster in the carboxy-terminal domain of polycystin-2. Binding to these adaptor proteins is regulated by the phosphorylation of polycystin-2 by the protein kinase casein kinase 2, required for the routing of polycystin-2 between ER, Golgi and plasma membrane compartments. Our paradigm that polycystin-2 is sorted to and active at both ER and plasma membrane reconciles the previously incongruent views of its localization and function. Furthermore, PACS proteins may represent a novel molecular mechanism for ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments." @default.
- W2022169605 created "2016-06-24" @default.
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- W2022169605 date "2005-02-03" @default.
- W2022169605 modified "2023-10-14" @default.
- W2022169605 title "Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation" @default.
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- W2022169605 doi "https://doi.org/10.1038/sj.emboj.7600566" @default.
- W2022169605 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/549624" @default.
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