Functional effects of the mouse weaver mutation on G protein-gated inwardly rectifying K+ channels

Neuron. 1996 Feb;16(2):321-31. doi: 10.1016/s0896-6273(00)80050-1.


The weaver mutation corresponds to a substitution of glycine to serine in the H5 region of a G protein-gated inwardly rectifying K+ channel gene (GIRK2). By studying mutant GIRK2 weaver homomultimeric channels and heteromultimeric channels comprised of GIRK2 weaver and GIRK1 in Xenopus oocytes, we found that GIRK2 weaver homomultimeric channels lose their selectivity for K+ ions, giving rise to inappropriate receptor-activated and basally active Na+ currents, whereas heteromultimers of GIRK2 weaver and GIRK1 appeared to have reduced current. Immunohistochemical localization indicates that GIRK2 and GIRK1 proteins are expressed in the cerebellar neurons of mice at postnatal day 4, at a time when these neurons normally undergo differentiation. Thus, the aberrant behavior of mutant GIRK2 weaver channels could affect the development of weaver mice in at least two distinct ways.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aging / metabolism
  • Animals
  • Animals, Newborn / growth & development
  • Animals, Newborn / metabolism
  • Cerebellum / metabolism
  • Electrophysiology
  • GTP-Binding Proteins / physiology*
  • Ion Channel Gating*
  • Mice
  • Mice, Neurologic Mutants
  • Oocytes / metabolism
  • Potassium Channels / genetics*
  • Potassium Channels / physiology*
  • Rats
  • Xenopus


  • Potassium Channels
  • GTP-Binding Proteins