Bahima Borràs, LaiaBalana, BartoszBodhinathan, KarthikTaura, JaumeTaylor, Natalie M.Nettleton, Margaret Y.Ciruela Alférez, FranciscoSlesinger, Paul A.2013-06-022013-06-022013-02-261932-6203https://hdl.handle.net/2445/43964G 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.8 p.application/pdfengcc-by (c) Bahima Borràs, Laia et al., 2013http://creativecommons.org/licenses/by/3.0/esProteïnes rasCanals de potassiProteïnes GRas proteinsPotassium channelsG Proteinsinfo:eu-repo/semantics/article6240602013-06-02info:eu-repo/semantics/openAccess23536889