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The weaver (wv) gene has been identified as a glycine to serine substitution at residue 156 in the H5 region of inwardly rectifying K+ channel, GIRK2. The mutation is permissive for the expression of homotetrameric channels that are nonselective for cations and G-protein-independent. Coexpression of GIRK2wv with GIRK1, GIRK2, or GIRK3 inXenopus oocytes along with expression of subunit combinations linked as dimers and tetramers was used to investigate the effects of the pore mutation on channel selectivity and gating as a function of relative subunit position and number within a heterotetrameric complex. GIRK1 formed functional, K+ selective channels with GIRK2 and GIRK3. Coexpression of GIRK2wv with GIRK1 gave rise to a component of K+-selective, G-protein-dependent current. Currents resulting from coexpression of GIRK2wvwith GIRK2 or GIRK3 were weaver-like. Current from dimers of GIRK1-GIRK2wv, GIRK2-GIRK2wv, and GIRK3-GIRK2wv was phenotypically similar to that obtained from coexpression of monomers. Linked tetramers containing GIRK1 and GIRK2wv in an alternating array gave rise to wild-type, K+-selective currents. When two mutant subunits were arranged adjacently in a tetramer, currents wereweaver-like. These results support the hypothesis that in specific channel stoichiometries, GIRK1 rescues theweaver phenotype and suggests a basis for the selective neuronal vulnerability that is observed in the weavermouse.

The Inwardly Rectifying K+Channel Subunit GIRK1 Rescues the GIRK2weaverPhenotype

The Inwardly Rectifying K⁺Channel Subunit GIRK1 Rescues the GIRK2weaverPhenotype