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Role of intrinsic disorder in muscle sarcomeres.
Tolkatchev, Dmitri; Smith, Garry E; Kostyukova, Alla S.
Affiliation
  • Tolkatchev D; Voiland School of Chemical Engineering & Bioengineering, Washington State University, Pullman, WA, United States. Electronic address: dmitri.tolkatchev@wsu.edu.
  • Smith GE; Voiland School of Chemical Engineering & Bioengineering, Washington State University, Pullman, WA, United States.
  • Kostyukova AS; Voiland School of Chemical Engineering & Bioengineering, Washington State University, Pullman, WA, United States.
Prog Mol Biol Transl Sci ; 166: 311-340, 2019.
Article in En | MEDLINE | ID: mdl-31521234
ABSTRACT
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sarcomeres / Tropomodulin / Intrinsically Disordered Proteins / Muscles Limits: Animals / Humans Language: En Journal: Prog Mol Biol Transl Sci Journal subject: BIOLOGIA MOLECULAR Year: 2019 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Sarcomeres / Tropomodulin / Intrinsically Disordered Proteins / Muscles Limits: Animals / Humans Language: En Journal: Prog Mol Biol Transl Sci Journal subject: BIOLOGIA MOLECULAR Year: 2019 Document type: Article