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PLoS One. 2013;8(3):e59800. doi: 10.1371/journal.pone.0059800. Epub 2013 Mar 25.

Ras-association domain of sorting Nexin 27 is critical for regulating expression of GIRK potassium channels.

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1
Peptide Biology Laboratories, The Salk Institute for Biological Studies, La Jolla, California, United States of America.

Abstract

G protein-gated inwardly rectifying potassium (GIRK) channels play an important role in regulating neuronal excitability. Sorting nexin 27b (SNX27b), which reduces surface expression of GIRK channels through a PDZ domain interaction, contains a putative Ras-association (RA) domain with unknown function. Deleting the RA domain in SNX27b (SNX27b-ΔRA) prevents the down-regulation of GIRK2c/GIRK3 channels. Similarly, a point mutation (K305A) in the RA domain disrupts regulation of GIRK2c/GIRK3 channels and reduces H-Ras binding in vitro. Finally, the dominant-negative H-Ras (S17N) occludes the SNX27b-dependent decrease in surface expression of GIRK2c/GIRK3 channels. Thus, the presence of a functional RA domain and the interaction with Ras-like G proteins comprise a novel mechanism for modulating SNX27b control of GIRK channel surface expression and cellular excitability.

PMID:
23536889
PMCID:
PMC3607560
DOI:
10.1371/journal.pone.0059800
[Indexed for MEDLINE]
Free PMC Article
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