ArticlePloS one2010
Ozz-E3 ubiquitin ligase targets sarcomeric embryonic myosin heavy chain during muscle development.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Unveiling muscle fatigue: identifying key gene biomarkers and therapeutic targets.Molecular and cellular biochemistry · 2026Article
- Mitochondrial proteostasis regulated by CRL5Communications biology · 2025Article
- Biophysical and functional study of CRL5Scientific reports · 2022Article
- Thick filament-associated myosin undergoes frequent replacement at the tip of the thick filament.FEBS open bio · 2022Article
- Multimodal human thymic profiling reveals trajectories and cellular milieu for T agonist selection.Frontiers in immunology · 2022Article
- Intramuscular injection of mesenchymal stem cells activates anabolic and catabolic systems in mouse skeletal muscle.Scientific reports · 2021Article
- The ubiquitin ligase Ozz decreases the replacement rate of embryonic myosin in myofibrils.Physiological reports · 2021Article
- The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease.International journal of molecular sciences · 2020Review
- UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.Nature communications · 2018Article
- Alix-mediated assembly of the actomyosin-tight junction polarity complex preserves epithelial polarity and epithelial barrier.Nature communications · 2016Article
- Skeletal muscle atrophy: disease-induced mechanisms may mask disuse atrophy.Journal of muscle research and cell motility · 2015Review
- Identification and characterization of the nano-sized vesicles released by muscle cells.FEBS letters · 2013Article
- Interferon-γ causes cardiac myocyte atrophy via selective degradation of myosin heavy chain in a model of chronic myocarditis.The American journal of pathology · 2012Article
- Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle.The Journal of biological chemistry · 2012Article
- A novel conserved isoform of the ubiquitin ligase UFD2a/UBE4B is expressed exclusively in mature striated muscle cells.PloS one · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
Muscle contractile proteins are expressed as a series of developmental isoforms that are in constant dynamic remodeling during embryogenesis, but how obsolete molecules are recognized and removed is not known. Ozz is a developmentally regulated protein that functions as the adaptor component of a RING-type ubiquitin ligase complex specific to striated muscle. Ozz(-/-) mutants exhibit defects in myofibrillogenesis and myofiber differentiation. Here we show that Ozz targets the rod portion of embryonic myosin heavy chain and preferentially recognizes the sarcomeric rather than the soluble pool of myosin. We present evidence that Ozz binding to the embryonic myosin isoform within sarcomeric thick filaments marks it for ubiquitination and proteolytic degradation, allowing its replacement with neonatal or adult isoforms. This unique function positions Ozz within a system that facilitates sarcomeric myosin remodeling during muscle maturation and regeneration. Our findings identify Ozz-E3 as the ubiquitin ligase complex that interacts with and regulates myosin within its fully assembled cytoskeletal structure.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.