Unc-1 Regulates Gap Junctions Important to Locomotion in C. Elegans.
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
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.
