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线虫秀丽隐杆线虫机械转导的分子建模

Molecular modeling of mechanotransduction in the nematode Caenorhabditis elegans.

作者信息

Tavernarakis N, Driscoll M

机构信息

Department of Molecular Biology and Biochemistry, Rutgers University, New Brunswick, New Jersey 08855, USA.

出版信息

Annu Rev Physiol. 1997;59:659-89. doi: 10.1146/annurev.physiol.59.1.659.

Abstract

Genetic and molecular studies of touch avoidance in the nematode Caenorhabditis elegans have resulted in a molecular model for a mechanotransducing complex. mec-4 and mec-10 encode proteins hypothesized to be subunits of a mechanically gated ion channel that are related to subunits of the vertebrate amiloride-sensitive epithelial Na+ channel. Products of mec-5, a novel collagen, and mec-9, a protein that includes multiple Kunitz-type protease inhibitor repeats and EGF repeats, may interact with the channel in the extracellular matrix. Inside the cell, specialized 15-protofilament microtubules composed of mec-12 alpha-tubulin and mec-7 beta-tubulin may be linked to the mechanosensitive channel by stomatin-homologous MEC-2. MEC-4 and MEC-10 are members of a large family of C. elegans proteins, the degenerins. Two other degenerins, UNC-8 and DEL-1, are candidate components of a stretch-sensitive channel in motor neurons. Implications for advancing understanding of mechanotransduction in other systems are discussed.

摘要

对线虫秀丽隐杆线虫中触觉回避的遗传和分子研究,已经得出了一个机械转导复合物的分子模型。mec-4和mec-10编码的蛋白质被假定为机械门控离子通道的亚基,这些亚基与脊椎动物氨氯地平敏感上皮钠通道的亚基相关。新型胶原蛋白mec-5和包含多个Kunitz型蛋白酶抑制剂重复序列和表皮生长因子重复序列的蛋白质mec-9的产物,可能在细胞外基质中与该通道相互作用。在细胞内部,由mec-12α-微管蛋白和mec-7β-微管蛋白组成的特殊15-原纤维微管,可能通过与stomatin同源的MEC-2与机械敏感通道相连。MEC-4和MEC-10是秀丽隐杆线虫蛋白质大家族——退化蛋白家族的成员。另外两种退化蛋白UNC-8和DEL-1,是运动神经元中拉伸敏感通道的候选组成部分。文中还讨论了这些研究对于推进其他系统中机械转导理解的意义。

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