A potassium channel-MiRP complex controls neurosensory function in Caenorhabditis elegans

Laura Bianchi, Suk Mei Kwok, Monica Driscoll, Federico Sesti

Research output: Contribution to journalArticlepeer-review

52 Scopus citations


MinK-related peptides (MiRPs) are single transmembrane proteins that associate with mammalian voltage-gated K+ subunits. Here we report the cloning and functional characterization of a MiRP β-subunit, MPS-1, and of a voltage-gated pore-forming potassium subunit, KVS-1, from the nematode Caenorhabditis elegans. mps-1 is expressed in chemosensory and mechanosensory neurons and co-localizes with kvs-1 in a subset of these. Inactivation of either mps-1 or kvs-1 by RNA interference (RNAi) causes partially overlapping neuronal defects and results in broad-spectrum neuronal dysfunction, including defective chemotaxis, disrupted mechanotransduction, and impaired locomotion. Inactivation of one subunit by RNAi dramatically suppresses the expression of the partner subunit only in cells where the two proteins co-localize. Co-expression of MPS-1 and KVS-1 in mammalian cells gives rise to a potassium current distinct from the KVS-1 current. Taken together these data indicate that potassium currents constitute a basic determinant for C. elegans neuronal function and unravel a unifying principle of evolutionary significance: that potassium channels in various organisms use MiRPs to generate uniqueness of function with rich variation in the details.

Original languageEnglish (US)
Pages (from-to)12415-12424
Number of pages10
JournalJournal of Biological Chemistry
Issue number14
StatePublished - Apr 4 2003
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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