Voiland School of Chemical Engineering & Bioengineering, Washington State University, Pullman, WA, United States.
Voiland School of Chemical Engineering & Bioengineering, Washington State University, Pullman, WA, United States.
Prog Mol Biol Transl Sci. 2019;166:311-340. doi: 10.1016/bs.pmbts.2019.03.014. Epub 2019 Apr 13.
The role and utility of intrinsically disordered regions (IDRs) is reviewed for two groups of sarcomeric proteins, such as members of tropomodulin/leiomodin (Tmod/Lmod) protein homology group and myosin binding protein C (MyBP-C). These two types of sarcomeric proteins represent very different but strongly interdependent functions, being responsible for maintaining structure and operation of the muscle sarcomere. The role of IDRs in the formation of complexes between thin filaments and Tmods/Lmods is discussed within the framework of current understanding of the thin filament length regulation. For MyBP-C, the function of IDRs is discussed in the context of MYBP-C-dependent sarcomere contraction and actomyosin activation.
本文综述了两个肌节蛋白组,即原肌球蛋白/肌联蛋白(Tmod/Lmod)蛋白同源组和肌球蛋白结合蛋白 C(MyBP-C)成员中,无规则区域(IDRs)的作用和功能。这两种类型的肌节蛋白代表了非常不同但相互依赖的功能,负责维持肌肉肌节的结构和功能。本文在当前对细肌丝长度调节的理解框架内,讨论了 IDRs 在细肌丝和 Tmod/Lmods 之间形成复合物中的作用。对于 MyBP-C,本文还讨论了 IDRs 在依赖于 MyBP-C 的肌节收缩和肌球蛋白激活中的功能。