Medical Journals

Unc-1 Regulates Gap Junctions Important to Locomotion in C. Elegans.

Authors:
  • Chen Bojun
  • Liu Qiang
  • Ge Qian
  • Xie Jia
  • Wang Zhao-Wen

From: Department of Neuroscience, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, Connecticut 06030.

Current biology : CB

  • Publish Date: Aug 2007
  • ISSN: 0960-9822
  • Volume: 17
  • Issue: 15
  • Pages: 1334-9
  • Medium: Print
  • Language: English
  • Citation (JAMA): Chen Bojun, Liu Qiang, Ge Qian, et al. Unc-1 Regulates Gap Junctions Important to Locomotion in C. Elegans.. Curr. Biol. Aug 2007;17:1334-9

Abstract

In C. elegans, loss-of-function (lf) mutations of the stomatin-like protein (SLP) UNC-1 and the innexin UNC-9 inhibit locomotion [1, 2] and modulate sensitivity to volatile anesthetics [3, 4]. It was unknown why unc-1(lf) and unc-9(lf) mutants have similar phenotypes. We tested the hypothesis that UNC-1 is a regulator of gap junctions formed by UNC-9. Analyses of junctional currents between body-wall muscle cells showed that electrical coupling was inhibited to a similar degree in unc-1(lf), unc-9(lf), and unc-1(lf);unc-9(lf) double mutants, suggesting that UNC-1 and UNC-9 function together. Expression of Punc-1::DsRED2 and Punc-9::GFP transcriptional fusions suggests that unc-1 and unc-9 are coexpressed in neurons and body-wall muscle cells. Immunohistochemistry showed that UNC-1 and UNC-9 colocalized at intercellular junctions and that unc-1(lf) did not alter UNC-9 expression or subcellular localization. Bimolecular fluorescence complementation (BiFC) assays suggest that UNC-1 and UNC-9 are physically very close at intercellular junctions. Targeted rescue experiments suggest that UNC-9 and UNC-1 function predominantly in neurons to control locomotion. Thus, in addition to the recently reported function of regulating mechanosensitive ion channels [5, 6], SLPs might have a novel function of regulating gap junctions.

Mesh Headings (Keywords): Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Gap Junctions, Locomotion, Membrane Proteins, Molecular Sequence Data, Muscle Cells, Neurons


Check for Full Text / PubMed Unique Identifier (PMID): 17658257


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