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A unique sorting nexin regulates trafficking of potassium channels via a PDZ domain interaction.

Authors: Lunn, ML  Nassirpour, R  Arrabit, C  Tan, J  McLeod, I  Arias, CM  Sawchenko, PE  Yates JR, 3RD  Slesinger, PA 
Citation: Lunn ML, etal., Nat Neurosci. 2007 Oct;10(10):1249-59. Epub 2007 Sep 2.
Pubmed: (View Article at PubMed) PMID:17828261
DOI: Full-text: DOI:10.1038/nn1953

G protein-gated potassium (Kir3) channels are important for controlling neuronal excitability in the brain. Using a proteomics approach, we have identified a unique rodent intracellular protein, sorting nexin 27 (SNX27), which regulates the trafficking of Kir3 channels. Like most sorting nexins, SNX27 possesses a functional PX domain that selectively binds the membrane phospholipid phosphatidylinositol-3-phosphate (PI3P) and is important for trafficking to the early endosome. SNX27, however, is the only sorting nexin to contain a PDZ domain. This PDZ domain discriminates between channels with similar class I PDZ-binding motifs, associating with the C-terminal end of Kir3.3 and Kir3.2c (-ESKV), but not with that of Kir2.1 (-ESEI) or Kv1.4 (-ETDV). SNX27 promotes the endosomal movement of Kir3 channels, leading to reduced surface expression, increased degradation and smaller Kir3 potassium currents. The regulation of endosomal trafficking via sorting nexins reveals a previously unknown mechanism for controlling potassium channel surface expression.

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CRRD Object Information
CRRD ID: 8554502
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.