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Huxleys’ Missing Filament: Form and Function of Titin in Vertebrate Striated Muscle
Annual Review of Physiology ( IF 15.7 ) Pub Date : 2017-02-13 00:00:00 , DOI: 10.1146/annurev-physiol-022516-034152
Stan Lindstedt 1 , Kiisa Nishikawa 2
Affiliation  

Although superthin filaments were inferred from early experiments on muscle, decades passed before their existence was accepted. Phylogenetic analyses suggest that titin, the largest known protein, first appeared in the common ancestor of chordates and nematodes and evolved rapidly via duplication. Twitchin and projectin evolved later by truncation. Sallimus mutants in Drosophila exhibit disrupted sarcomere and chromosome structure, suggesting that giant proteins may have evolved as chromosomal scaffolds that were co-opted for a similar purpose in striated muscles. Though encoded by only one gene, titin comprises hundreds of exons and has the potential for enormous diversity. Shorter isoforms typically confer greater passive stiffness associated with smaller in vivo muscle strains. Recent studies demonstrate unequivocally that titin stiffness increases upon muscle activation, but the mechanisms are only now being uncovered. Although some basic principles have been established, a vast opportunity remains to extend our understanding of titin function in striated muscle.

中文翻译:


赫x黎的缺失细丝:脊椎动物横纹肌中的丁丁的形式和功能

尽管超细细丝是从早期的肌肉实验中推断出来的,但几十年来,它们的存在才被人们接受。系统发育分析表明,已知最大的蛋白titin首先出现在弦和线虫的共同祖先中,并通过复制而迅速进化。Twitchin和projectin后来通过截短而进化。果蝇中的Sallimus突变体表现出破坏的肌节和染色体结构,这表明巨蛋白可能已经进化为染色体支架,它们被横纹肌用于相似的目的。尽管仅由一个基因编码,但titin包含数百个外显子,并具有巨大的多样性。较短的同工型通常会产生与较小的体内肌肉劳损相关的更大的被动刚度。最近的研究清楚地表明,肌动蛋白的刚度会随着肌肉的激活而增加,但是这种机制目前才被发现。尽管已经建立了一些基本原理,但是仍然存在大量的机会来扩展我们对横纹肌肌动蛋白功能的理解。

更新日期:2017-02-13
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