Myomesin 3, a Novel Structural Component of the M-band in Striated Muscle

Schoenauer, Roman; Lange, Stephan; Hirschy, Alain; Ehler, Elisabeth; Perriard, Jean‐Claude; Agarkova, Irina

doi:10.1016/j.jmb.2007.11.048

Cited by 77 publications

(87 citation statements)

References 34 publications

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“…4D-G) raise the possibility that thick filament components may partially assemble with these structures. Therefore, we immunostained embryonic hearts for myomesin, a marker of thick filament assembly that crosslinks myosin thick filaments at the M-line Schoenauer et al, 2005;Schoenauer et al, 2008). In the myofibrils of αTM1 +/+ hearts, myomesin localized at the M-line in the middle of the sarcomere, exhibiting a striated pattern of staining alternating with α-actinin at the Z-line, as expected (Fig.…”

Section: αTm1-deficient Cardiomyocytes Assemble Aberrant F-actin Fibrsupporting

confidence: 61%

Tropomyosin is required for cardiac morphogenesis, myofibril assembly, and formation of adherens junctions in the developing mouse embryo

McKeown¹,

Nowak²,

Gokhin³

et al. 2014

Developmental Dynamics

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Section: αTm1-deficient Cardiomyocytes Assemble Aberrant F-actin Fibrsupporting

confidence: 61%

Tropomyosin is required for cardiac morphogenesis, myofibril assembly, and formation of adherens junctions in the developing mouse embryo

McKeown¹,

Nowak²,

Gokhin³

et al. 2014

Developmental Dynamics

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“…This ability of My13 to mediate antiparallel dimerisation is shared between all MYOM isoforms. However, despite the high homology of the My13 domains in myomesin, M-protein and myomesin-3, there is no evidence for heterodimer formation (Schoenauer et al, 2008), suggesting that each myomesin form fulfils separate and distinct functions. The interaction of the N-terminal myosin-binding domain is not yet fully understood: this region is highly divergent between the three myomesin isoforms, possibly reflecting their different positions in the bare zone of the myosin filament, and contains multiple phosphorylation sites indicative of dynamic regulation.…”

Section: M-band Cytoskeleton: All's Well That Ends Wellmentioning

confidence: 96%

“…The known integral sarcomeric cytoskeleton proteins of the Mband comprise three closely related M-band proteins: myomesin-1, M-protein (myomesin-2) and myomesin-3 that are encoded by three mammalian MYOM genes (Schoenauer et al, 2008). In addition, titin, the giant protein obscurin and obsl1 are involved in organising the transverse crosslinks between myosin filaments that are essential to maintain the axial alignment of adjacent myosin filaments.…”

Section: M-band Cytoskeleton: All's Well That Ends Wellmentioning

confidence: 99%

“…Myomesin isoforms correlate with the contractile properties in different fibre types: while myomesin-1 is constitutively expressed in all striated muscles, myomesin-2 is expressed only in the adult heart and fast fibres, whereas myomesin-3 is expressed in skeletal muscle intermediate fibre types (Agarkova et al, 2004;Schoenauer et al, 2011Schoenauer et al, , 2008. Of the three MYOM isogenes, MYOM1 appears to be the one that is essential in all muscle types: not only is it constitutively co-expressed with other myomesins but also the cellular knockdown of myomesin-1 completely disrupts myofibril integrity (Fukuzawa et al, 2008).…”

Section: M-band Cytoskeleton: All's Well That Ends Wellmentioning

confidence: 99%

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The sarcomeric cytoskeleton: from molecules to motion

Gautel

Djinović-Carugo

2016

Journal of Experimental Biology

194

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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“…Differential accumulation in slow versus fast muscles was also found for Mband proteins that are required for the regular packing and organization of thick filaments. So far, three Myomesins, namely Myomesin-1 (also known as Skelemin or EH-myomesin) (36), Myomesin-2 (also known as M-protein) (37), and Myomesin-3 (38) have been localized to the M-band. Our results supported previous findings that Myomesin-2 is predominantly located in fast (EDL) and Myomesin-3 in slow muscles (soleus).…”

Section: Silac-assisted Mass Spectrometry Greatly Increases the Numbementioning

confidence: 99%

On Marathons and Sprints: An Integrated Quantitative Proteomics and Transcriptomics Analysis of Differences Between Slow and Fast Muscle Fibers

Drexler

Ruhs

Konzer

et al. 2012

Molecular & Cellular Proteomics

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Skeletal muscle tissue contains slow as well as fast twitch muscle fibers that possess different metabolic and contractile properties. Although the distribution of individual proteins in fast and slow fibers has been investigated extensively, a comprehensive proteomic analysis, which is key for any systems biology approach to muscle tissues, is missing. Here, we compared the global protein levels and gene expression profiles of the predominantly slow soleus and fast extensor digitorum longus muscles using the principle of in vivo stable isotope labeling with amino acids based on a fully lysine-6 labeled SILAC-mouse. We identified 551 proteins with significant quantitative differences between slow soleus and fast extensor digitorum longus fibers out of >2000 quantified proteins, which greatly extends the repertoire of proteins differentially regulated between both muscle types. Most of the differentially regulated proteins mediate cellular contraction, ion homeostasis, glycolysis, and oxidation, which reflect the major functional differences between both muscle types. Comparison of proteomics and transcriptomics data uncovered the existence of fiber-type specific posttranscriptional regulatory mechanisms resulting in differential accumulation of Myosin-8 and ␣-protein kinase 3 proteins and mRNAs among others. Phosphoproteome analysis of soleus and extensor digitorum longus muscles identified 2573 phosphosites on 973 proteins including 1040 novel phosphosites. The in vivo stable isotope labeling with amino acids-mouse approach used in our study provides a comprehensive view into the protein networks that direct fiber-type specific functions and allows a detailed dissection of the molecular composition of slow and fast muscle tissues with unprecedented Skeletal muscles contain different types of fibers, which are responsible for specific biological properties and functions of individual muscles. Muscle fibers have been classified into slow type I and fast type II fibers mainly based on myofibrillar ATP staining and immunohistochemistry using specific antibodies (1).Slow type I fibers show a red tint, contain high numbers of mitochondria, and their energy supply is mainly based on oxidative metabolism. These features enable slow fibers to execute long lasting contractions, which are essential for the maintenance of body posture. The primary function of type II fibers is the rapid contraction of muscles. Fast fibers are divided into three additional subclasses: Type IIb and IIx (also known as IId) are glycolytic fibers, whereas type IIa fibers are more comparable to oxidative type I fibers (2). Type II fibers, which mainly derive their energy from glycolysis, are thus more susceptible to fatigue compared with Type I fibers.Muscle fibers have also been classified based on the expression of different isoforms of myosin heavy chain (MyHC) proteins. Myosins are the major contractile proteins and their activation by ATP and Ca 2ϩ ions results in shortening of muscle fibers. For example, slow type I fibers express MyHCI␤ a...

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Myomesin 3, a Novel Structural Component of the M-band in Striated Muscle

Cited by 77 publications

References 34 publications

Tropomyosin is required for cardiac morphogenesis, myofibril assembly, and formation of adherens junctions in the developing mouse embryo

Tropomyosin is required for cardiac morphogenesis, myofibril assembly, and formation of adherens junctions in the developing mouse embryo

The sarcomeric cytoskeleton: from molecules to motion

On Marathons and Sprints: An Integrated Quantitative Proteomics and Transcriptomics Analysis of Differences Between Slow and Fast Muscle Fibers

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