Dimerisation of Myomesin: Implications for the Structure of the Sarcomeric M-band

Lange, Stephan; Himmel, Mirko; Auerbach, Daniel; Agarkova, Irina; Hayeß, K.; Fürst, Dieter O.; Perriard, Jean‐Claude; Ehler, Elisabeth

doi:10.1016/j.jmb.2004.10.040

Cited by 69 publications

(69 citation statements)

References 42 publications

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“…It was found that myomesin binds to myosin by means of the first N-terminal domain and to titin domain m4 by three Fn-like domains, My4-My6 [18], while the last C-terminal domain, My13, has the ability to undergo antiparallel dimerization [30] (Figure 2). These data, combined with the previous EM observations (Box 1), resulted in a novel 3D model of myomesin incorporation into the M-band [30] (Figure 3). In this, the link between myosin filaments is provided by antiparallel dimers of myomesin molecules that interact end-to-end via the last C-terminal domain and bind to the thick filaments by their N-terminal domains.…”

Section: Trends In Cell Biologymentioning

confidence: 99%

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The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere

Agarkova¹,

Perriard²

2005

Trends in Cell Biology

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204

205

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Section: Trends In Cell Biologymentioning

confidence: 99%

“…Similar to the PEVK fragment of titin, the EH-fragment is mostly unfolded and functions like an entropic spring [31] (Box 2). Phosphorylation sites (P, blue circles) [18,19] and interacting partners (identified above brackets) [11,18,30,69] are indicated.…”

Section: Trends In Cell Biologymentioning

confidence: 99%

The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere

Agarkova¹,

Perriard²

2005

Trends in Cell Biology

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204

205

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“…10 In addition to the strategic localization and mechanical spring function, titin also acts as a length-dependent sensor during stretch and promotes actin-myosin interaction. 11 Titin is stabilized by the cross-linking protein telethonin (T-Cap), which localizes at the Z-line and is also part of titin sensor machinery (Figure 1). 12 The complex protein interactions in the sarcomere entwine telethonin to other Z-line components through the family of the telethonin-binding proteins of the Z-disc, FATZ, also known as calsarcin and myozenin.…”

Section: The Sarcomerementioning

confidence: 99%

Cytoskeletal Basis of Ion Channel Function in Cardiac Muscle

Vatta

Faulkner

2006

Future Cardiol.

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SummaryThe heart is a force-generating organ that responds to self-generated electrical stimuli from specialized cardiomyocytes. This function is modulated by sympathetic and parasympathetic activity.In order to contract and accommodate the repetitive morphological changes induced by the cardiac cycle, cardiomyocytes depend on their highly evolved and specialized cytoskeletal apparatus. Defects in components of the cytoskeleton, in the long term, affect the ability of the cell to compensate at both functional and structural levels. In addition to the structural remodeling, the myocardium becomes increasingly susceptible to altered electrical activity leading to arrhythmogenesis. The development of arrhythmias secondary to structural remodeling defects has been noted, although the detailed molecular mechanisms are still elusive. Here I will review the current knowledge of the molecular and functional relationships between the cytoskeleton and ion channels and, I will discuss the future impact of new data on molecular cardiology research and clinical practice.

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“…These domains confer specificity to ligand interactions and the stability required for Agarkova et al, 2003), whose molecular identity is still unclear; a model for their possible molecular interpretation was proposed by Lange et al (2005a). Large circles, myosin filaments; small circles, components of the linking filaments.…”

Section: Introductionmentioning

confidence: 99%

The sarcomeric cytoskeleton: from molecules to motion

Gautel

Djinović-Carugo

2016

Journal of Experimental Biology

192

177

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Highly ordered organisation of striated muscle is the prerequisite for the fast and unidirectional development of force and motion during heart and skeletal muscle contraction. A group of proteins, summarised as the sarcomeric cytoskeleton, is essential for the ordered assembly of actin and myosin filaments into sarcomeres, by combining architectural, mechanical and signalling functions. This review discusses recent cell biological, biophysical and structural insight into the regulated assembly of sarcomeric cytoskeleton proteins and their roles in dissipating mechanical forces in order to maintain sarcomere integrity during passive extension and active contraction. α-Actinin crosslinks in the Z-disk show a pivot-and-rod structure that anchors both titin and actin filaments. In contrast, the myosin crosslinks formed by myomesin in the M-band are of a balland-spring type and may be crucial in providing stable yet elastic connections during active contractions, especially eccentric exercise.

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Dimerisation of Myomesin: Implications for the Structure of the Sarcomeric M-band

Cited by 69 publications

References 42 publications

The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere

The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere

Cytoskeletal Basis of Ion Channel Function in Cardiac Muscle

The sarcomeric cytoskeleton: from molecules to motion

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