Maryon E B, Coronado R, Anderson P
Department of Genetics, University of Wisconsin, Madison 53706, USA.
J Cell Biol. 1996 Aug;134(4):885-93. doi: 10.1083/jcb.134.4.885.
Striated muscle contraction is elicited by the release of stored calcium ions through ryanodine receptor channels in the sarcoplasmic reticulum. ryr-1 is a C. elegans ryanodine receptor homologue that is expressed in body-wall muscle cells used for locomotion. Using genetic methods, we show that ryr-1 is the previously identified locus unc-68. First, transposon-induced deletions within ryr-1 are alleles of unc-68. Second, transformation of unc-68 mutants with ryr-1 genomic DNA results in rescue of the Unc phenotype. unc-68 mutants move poorly, exhibiting an incomplete flaccid paralysis, yet have normal muscle ultrastructure. The mutants are insensitive to the paralytic effects of ryanodine, and lack detectable ryanodine-binding activity. The Unc-68 phenotype suggests that ryanodine receptors are not essential for excitation-contraction coupling in nematodes, but act to amplify a (calcium) signal that is sufficient for contraction.
横纹肌收缩是由肌浆网中通过雷诺丁受体通道释放储存的钙离子引发的。ryr-1是秀丽隐杆线虫的雷诺丁受体同源物,在用于运动的体壁肌肉细胞中表达。我们通过遗传学方法表明,ryr-1就是先前鉴定出的unc-68基因座。首先,ryr-1内转座子诱导的缺失是unc-68的等位基因。其次,用ryr-1基因组DNA转化unc-68突变体可挽救Unc表型。unc-68突变体运动能力差,表现出不完全的弛缓性麻痹,但肌肉超微结构正常。这些突变体对雷诺丁的麻痹作用不敏感,且缺乏可检测到的雷诺丁结合活性。Unc-68表型表明,雷诺丁受体对线虫的兴奋-收缩偶联并非必不可少,但起到放大足以引发收缩的(钙)信号的作用。