An Alpha-Catulin Homologue Controls Neuromuscular Function through Localization of the Dystrophin Complex and BK Channels in Caenorhabditis elegans

被引：27
作者：
Abraham, Linu S. [1 ]
Oh, Hyun J. [1 ]
Sancar, Feyza [2 ]
Richmond, Janet E. [2 ]
Kim, Hongkyun [1 ]
机构：
[1] Rosalind Franklin Univ Med & Sci, Chicago Med Sch, Dept Cell Biol & Anat, N Chicago, IL USA
[2] Univ Illinois, Dept Biol Sci, Chicago, IL 60680 USA
来源：
PLOS GENETICS | 2010年 / 6卷 / 08期
关键词：
CA2+-ACTIVATED K+ CHANNELS; POTASSIUM CHANNEL; C-ELEGANS; PYRAMIDAL NEURONS; ION CHANNELS; DYSTROBREVIN; VINCULIN; BINDING; CHROMAFFIN; EXPRESSION;
D O I：
10.1371/journal.pgen.1001077
中图分类号：
Q3 [遗传学];
学科分类号：
071007 ; 090102 ;
摘要：
The large conductance, voltage- and calcium-dependent potassium (BK) channel serves as a major negative feedback regulator of calcium-mediated physiological processes and has been implicated in muscle dysfunction and neurological disorders. In addition to membrane depolarization, activation of the BK channel requires a rise in cytosolic calcium. Localization of the BK channel near calcium channels is therefore critical for its function. In a genetic screen designed to isolate novel regulators of the Caenorhabditis elegans BK channel, SLO-1, we identified ctn-1, which encodes an alpha-catulin homologue with homology to the cytoskeletal proteins a-catenin and vinculin. ctn-1 mutants resemble slo-1 loss-of-function mutants, as well as mutants with a compromised dystrophin complex. We determined that CTN-1 uses two distinct mechanisms to localize SLO-1 in muscles and neurons. In muscles, CTN-1 utilizes the dystrophin complex to localize SLO-1 channels near L-type calcium channels. In neurons, CTN-1 is involved in localizing SLO-1 to a specific domain independent of the dystrophin complex. Our results demonstrate that CTN-1 ensures the localization of SLO-1 within calcium nanodomains, thereby playing a crucial role in muscles and neurons.
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页数：13
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