ArticleJournal of muscle research and cell motility1999
Thick filament assembly occurs after the formation of a cytoskeletal scaffold.
Article in Journal of muscle research and cell motility, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 59 citations in OpenAlex.
- The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathy.The Journal of general physiology · 2016Article
- Reduced passive force in skeletal muscles lacking protein arginylation.American journal of physiology. Cell physiology · 2016Article
- α-Synemin localizes to the M-band of the sarcomere through interaction with the M10 region of titin.FEBS letters · 2014Article
- Getting folded: chaperone proteins in muscle development, maintenance and disease.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- Cardiomyopathy mutations in the tail of β-cardiac myosin modify the coiled-coil structure and affect integration into thick filaments in muscle sarcomeres in adult cardiomyocytes.The Journal of biological chemistry · 2013Article
- Heavy and light roles: myosin in the morphogenesis of the heart.Cellular and molecular life sciences : CMLS · 2013Review
- Sarcomere formation occurs by the assembly of multiple latent protein complexes.PLoS genetics · 2010Article
- Molecular cloning and expression profile analysis of porcine TCAP gene.Molecular biology reports · 2010Article
- Muscle giants: molecular scaffolds in sarcomerogenesis.Physiological reviews · 2009Review
- The initial steps of myofibril assembly: integrins pave the way.Nature reviews. Molecular cell biology · 2009Review
- The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis.Development (Cambridge, England) · 2008Article
- Secondary and tertiary structure elasticity of titin Z1Z2 and a titin chain model.Biophysical journal · 2007Article
- Mef2s are required for thick filament formation in nascent muscle fibres.Development (Cambridge, England) · 2007Article
- Depletion of zebrafish titin reduces cardiac contractility by disrupting the assembly of Z-discs and A-bands.Circulation research · 2007Article
- M line-deficient titin causes cardiac lethality through impaired maturation of the sarcomere.The Journal of cell biology · 2006Article
- Essential role of obscurin in cardiac myofibrillogenesis and hypertrophic response: evidence from small interfering RNA-mediated gene silencing.Histochemistry and cell biology · 2006Article
- Microtubule-dependent transport and organization of sarcomeric myosin during skeletal muscle differentiation.The EMBO journal · 2005Article
- The mode of myofibril remodelling in human skeletal muscle affected by DOMS induced by eccentric contractions.Histochemistry and cell biology · 2003Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The development of myofibrils involves the formation of contractile filaments and their assembly into the strikingly regular structure of the sarcomere. We analysed this assembly process in cultured human skeletal muscle cells and in rat neonatal cardiomyocytes by immunofluorescence microscopy using antibodies directed against cytoskeletal and contractile proteins. In particular, the question in which temporal order the respective proteins are integrated into developing sarcomeres was addressed. Although sarcomeric myosin heavy chain is expressed as one of the first myofibrillar proteins, its characteristic A band arrangement is reached at a very late stage. In contrast, titin, then myomesin and finally C-protein (MyBP-C) gradually form a regularly arranged scaffold on stress fiber-like structures (SFLS), on non-striated myofibrils (NSMF) and on nascent striated myofibrils (naSMF). Immediately subsequent to the completion of sarcomere cytoskeleton formation, the labeling pattern of myosin changes from the continuous staining of SFLS to the periodic staining characteristic for mature myofibrils. This series of events can be seen most clearly in the skeletal muscle cell cultures and--probably due to a faster developmental progression less well in cardiomyocytes. We therefore conclude that the correct assembly of a cytoskeletal scaffold is a prerequisite for correct thick filament assembly and for the integration of the contractile apparatus into the myofibril.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.