Title:
|
Ras-association domain of sorting nexin 27 is critical for regulating expression of GIRK potassium channels
|
Author:
|
Bahima Borràs, Laia; Balana, Bartosz; Bodhinathan, Karthik; Taura, Jaume; Taylor, Natalie M.; Nettleton, Margaret Y.; Ciruela Alférez, Francisco; Slesinger, Paul A.
|
Other authors:
|
Universitat de Barcelona |
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-DRA) 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. |
Subject(s):
|
-Proteïnes ras -Canals de potassi -Proteïnes G -Ras proteins -Potassium channels -G Proteins |
Rights:
|
cc-by (c) Bahima Borràs, Laia et al., 2013
http://creativecommons.org/licenses/by/3.0/es |
Document type:
|
Article Article - Published version |
Published by:
|
Public Library of Science (PLoS)
|
Share:
|
|