Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology

McNamara, James W.; Sadayappan, Sakthivel

doi:10.1016/j.abb.2018.10.007

Cited by 34 publications

(33 citation statements)

References 102 publications

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“…This light chain in all muscles can be reversibly phosphorylated and this also has a modulatory effect on activation even in vertebrate striated muscles [69,70]. In vertebrate cardiac muscles, C-protein (MyBP-C) can also be phosphorylated and it too can modulate the contractile response [71,72].…”

Section: Striated Muscle Sarcomeres and The Contractile Mechanismmentioning

confidence: 99%

Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview

Squire

2019

IJMS

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Muscular contraction is a fundamental phenomenon in all animals; without it life as we know it would be impossible. The basic mechanism in muscle, including heart muscle, involves the interaction of the protein filaments myosin and actin. Motility in all cells is also partly based on similar interactions of actin filaments with non-muscle myosins. Early studies of muscle contraction have informed later studies of these cellular actin-myosin systems. In muscles, projections on the myosin filaments, the so-called myosin heads or cross-bridges, interact with the nearby actin filaments and, in a mechanism powered by ATP-hydrolysis, they move the actin filaments past them in a kind of cyclic rowing action to produce the macroscopic muscular movements of which we are all aware. In this special issue the papers and reviews address different aspects of the actin-myosin interaction in muscle as studied by a plethora of complementary techniques. The present overview provides a brief and elementary introduction to muscle structure and function and the techniques used to study it. It goes on to give more detailed descriptions of what is known about muscle components and the cross-bridge cycle using structural biology techniques, particularly protein crystallography, electron microscopy and X-ray diffraction. It then has a quick look at muscle mechanics and it summarises what can be learnt about how muscle works based on the other studies covered in the different papers in the special issue. A picture emerges of the main molecular steps involved in the force-producing process; steps that are also likely to be seen in non-muscle myosin interactions with cellular actin filaments. Finally, the remarkable advances made in studying the effects of mutations in the contractile assembly in causing specific muscle diseases, particularly those in heart muscle, are outlined and discussed.

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Section: Striated Muscle Sarcomeres and The Contractile Mechanismmentioning

confidence: 99%

Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview

Squire

2019

IJMS

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“…However, it is not yet clear which mechanisms regulate the formation of pathological and functional amyloids in the organism. Research into the amyloid properties of multidomain muscle proteins, such as titin and myosin binding protein-C (MyBP-C), which consist of β-folded domains [ 12 , 13 , 14 ], can, in our mind, contribute to the insight into this problem.…”

Section: Introductionmentioning

confidence: 99%

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro

Bobyleva

Shumeyko

Yakupova

et al. 2021

IJMS

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This work investigated in vitro aggregation and amyloid properties of skeletal myosin binding protein-C (sMyBP-C) interacting in vivo with proteins of thick and thin filaments in the sarcomeric A-disc. Dynamic light scattering (DLS) and transmission electron microscopy (TEM) found a rapid (5–10 min) formation of large (>2 μm) aggregates. sMyBP-C oligomers formed both at the initial 5–10 min and after 16 h of aggregation. Small angle X-ray scattering (SAXS) and DLS revealed sMyBP-C oligomers to consist of 7–10 monomers. TEM and atomic force microscopy (AFM) showed sMyBP-C to form amorphous aggregates (and, to a lesser degree, fibrillar structures) exhibiting no toxicity on cell culture. X-ray diffraction of sMyBP-C aggregates registered reflections attributed to a cross-β quaternary structure. Circular dichroism (CD) showed the formation of the amyloid-like structure to occur without changes in the sMyBP-C secondary structure. The obtained results indicating a high in vitro aggregability of sMyBP-C are, apparently, a consequence of structural features of the domain organization of proteins of this family. Formation of pathological amyloid or amyloid-like sMyBP-C aggregates in vivo is little probable due to amino-acid sequence low identity (<26%), alternating ordered/disordered regions in the protein molecule, and S–S bonds providing for general stability.

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“…One protein group, comprising skeletal and cardiac isoforms of myosin-binding protein C (MyBP-C), is recognized as having a regulatory role in sarcomere contraction. [2][3][4] Another protein group consists of several isoforms of tropomodulin/leiomodin homology family, and it is known to regulate thin filament formation. 2,[5][6][7] Both groups represent two different yet strongly related aspects of atomic force microscopy (AFM) was consistent with both PAL and M-domain being at least partially unfolded and lacking a well-defined three-dimensional structure.…”

Section: Introductionmentioning

confidence: 99%

Role of intrinsic disorder in muscle sarcomeres

Tolkatchev

Smith

Kostyukova

2019

Progress in Molecular Biology and Translational Science

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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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Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology

Cited by 34 publications

References 102 publications

Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview

Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro

Role of intrinsic disorder in muscle sarcomeres

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