Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/43964
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 J.
Taylor, Natalie M.
Nettleton, Margaret Y.
Ciruela Alférez, Francisco
Slesinger, Paul A.
Keywords: Proteïnes ras
Canals de potassi
Proteïnes G
Ras proteins
Potassium channels
G Proteins
Issue Date: 26-Feb-2013
Publisher: Public Library of Science (PLoS)
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.
It is part of: PLoS One, 2013, vol. 8, num. 3, p. e59800
URI: http://hdl.handle.net/2445/43964
ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Institut d'lnvestigació Biomèdica de Bellvitge (IDIBELL))
Articles publicats en revistes (Patologia i Terapèutica Experimental)

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