Literature DB >> 31521234

Role of intrinsic disorder in muscle sarcomeres.

Dmitri Tolkatchev1, Garry E Smith2, Alla S Kostyukova2.   

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.
© 2019 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Actin; Intrinsically disordered region; Leiomodin; Myosin; Myosin binding protein C; Sarcomere; Thick filament; Thin filament; Tropomodulin; Tropomyosin

Mesh:

Substances:

Year:  2019        PMID: 31521234      PMCID: PMC7134574          DOI: 10.1016/bs.pmbts.2019.03.014

Source DB:  PubMed          Journal:  Prog Mol Biol Transl Sci        ISSN: 1877-1173            Impact factor:   3.622


  108 in total

1.  Folding properties of functional domains of tropomodulin.

Authors:  A S Kostyukova; E I Tiktopulo; Y Maéda
Journal:  Biophys J       Date:  2001-07       Impact factor: 4.033

2.  Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C.

Authors:  F Steven Korte; Kerry S McDonald; Samantha P Harris; Richard L Moss
Journal:  Circ Res       Date:  2003-09-18       Impact factor: 17.367

3.  Structural insight into unique cardiac myosin-binding protein-C motif: a partially folded domain.

Authors:  Jack W Howarth; Srinivas Ramisetti; Kristof Nolan; Sakthivel Sadayappan; Paul R Rosevear
Journal:  J Biol Chem       Date:  2012-01-10       Impact factor: 5.157

4.  Mechanical unfolding of cardiac myosin binding protein-C by atomic force microscopy.

Authors:  Arpád Karsai; Miklós S Z Kellermayer; Samantha P Harris
Journal:  Biophys J       Date:  2011-10-19       Impact factor: 4.033

5.  The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner.

Authors:  Justin F Shaffer; Robert W Kensler; Samantha P Harris
Journal:  J Biol Chem       Date:  2009-03-05       Impact factor: 5.157

6.  Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy.

Authors:  Pascale Richard; Philippe Charron; Lucie Carrier; Céline Ledeuil; Theary Cheav; Claire Pichereau; Abdelaziz Benaiche; Richard Isnard; Olivier Dubourg; Marc Burban; Jean-Pierre Gueffet; Alain Millaire; Michel Desnos; Ketty Schwartz; Bernard Hainque; Michel Komajda
Journal:  Circulation       Date:  2003-04-21       Impact factor: 29.690

7.  Tropomodulin contains two actin filament pointed end-capping domains.

Authors:  Velia M Fowler; Norma J Greenfield; Jeannette Moyer
Journal:  J Biol Chem       Date:  2003-07-14       Impact factor: 5.157

8.  Functional differences between the N-terminal domains of mouse and human myosin binding protein-C.

Authors:  Justin F Shaffer; Peony Wong; Kristina L Bezold; Samantha P Harris
Journal:  J Biomed Biotechnol       Date:  2010-04-07

9.  Leiomodin is an actin filament nucleator in muscle cells.

Authors:  David Chereau; Malgorzata Boczkowska; Aneta Skwarek-Maruszewska; Ikuko Fujiwara; David B Hayes; Grzegorz Rebowski; Pekka Lappalainen; Thomas D Pollard; Roberto Dominguez
Journal:  Science       Date:  2008-04-11       Impact factor: 47.728

10.  Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosin for assembly.

Authors:  C C Gregorio; V M Fowler
Journal:  J Cell Biol       Date:  1995-05       Impact factor: 10.539

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  1 in total

1.  Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.

Authors:  Dmitri Tolkatchev; Garry E Smith; Lauren E Schultz; Mert Colpan; Gregory L Helms; John R Cort; Carol C Gregorio; Alla S Kostyukova
Journal:  PLoS Biol       Date:  2020-09-08       Impact factor: 8.029

  1 in total

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