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cc-by (c) Bahima Borràs, Laia et al., 2013
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/43964

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

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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.

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BAHIMA BORRÀS, Laia, et al. Ras-association domain of sorting nexin 27 is critical for regulating expression of GIRK potassium channels. PLoS One. 2013. Vol. 8, num. 3, pags. e59800. ISSN 1932-6203. [consulted: 10 of June of 2026]. Available at: https://hdl.handle.net/2445/43964

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