ArticleThe EMBO journal1997
Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
86 citing papers in PubMed, 233 citations in OpenAlex.
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- MYH7 in cardiomyopathy and skeletal muscle myopathy.Molecular and cellular biochemistry · 2024Review
- Bi-allelic variants of FILIP1 cause congenital myopathy, dysmorphism and neurological defects.Brain : a journal of neurology · 2023Article
- Structure determination and analysis of titin A-band fibronectin type III domains provides insights for disease-linked variants and protein oligomerisation.Journal of structural biology · 2023Article
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- A Novel Nonsense PathogenicCurrent issues in molecular biology · 2023Article
- Time-resolved phosphoproteome and proteome analysis reveals kinase signaling on master transcription factors during myogenesis.iScience · 2022Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Thick filament-associated myosin undergoes frequent replacement at the tip of the thick filament.FEBS open bio · 2022Article
- The role of the M-band myomesin proteins in muscle integrity and cardiac disease.Journal of biomedical science · 2022Review
- Targeted transcript analysis in muscles from patients with genetically diverse congenital myopathies.Brain communications · 2022Article
- Natural variant frequencies across domains from different sarcomere proteins cross-correlate to identify inter-protein contacts associated with cardiac muscle function and disease.Molecular biomedicine · 2021Article
- The ubiquitin ligase Ozz decreases the replacement rate of embryonic myosin in myofibrils.Physiological reports · 2021Article
- Contiguity and Structural Impacts of a Non-Myosin Protein within the Thick Filament Myosin Layers.Biology · 2021Article
- Myofiber androgen receptor increases muscle strength mediated by a skeletal muscle splicing variant of Mylk4.iScience · 2021Article
- Knockout of MYOM1 in human cardiomyocytes leads to myocardial atrophy via impairing calcium homeostasis.Journal of cellular and molecular medicine · 2021Article
- Proteomic Studies on the Mechanism of Myostatin Regulating Cattle Skeletal Muscle Development.Frontiers in genetics · 2021Article
- Identification ofDisease models & mechanisms · 2020Article
- MuRF1/TRIM63, Master Regulator of Muscle Mass.International journal of molecular sciences · 2020Review
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The M band of sarcomeric muscle is a highly complex structure which contributes to the maintenance of the regular lattice of thick filaments. We propose that the spatial coordination of this assembly is regulated by specific interactions of myosin filaments, the M band protein myomesin and the large carboxy-terminal region of titin. Corresponding binding sites between these proteins were identified. Myomesin binds myosin in the central region of light meromyosin (LMM, myosin residues 1506-1674) by its unique amino-terminal domain My1. A single titin immunoglobulin domain, m4, interacts with a myomesin fragment spanning domains My4-My6. This interaction is regulated by phosphorylation of Ser482 in the linker between myomesin domains My4 and My5. Myomesin phosphorylation at this site by cAMP-dependent kinase and similar or identical activities in muscle extracts block the association with titin. We propose that this demonstration of a phosphorylation-controlled interaction in the sarcomeric cytoskeleton is of potential relevance for sarcomere formation and/or turnover. It also reveals how binding affinities of modular proteins can be regulated by modifications of inter-domain linkers.
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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.