ArticleBiochemical and biophysical research communications2010
Drosophila UNC-45 prevents heat-induced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase.
Article in Biochemical and biophysical research communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 35 citations in OpenAlex.
- Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Review
- Disruption of Drosophila larval muscle structure and function by UNC45 knockdown.BMC molecular and cell biology · 2021Article
- Under construction: The dynamic assembly, maintenance, and degradation of the cardiac sarcomere.Journal of molecular and cellular cardiology · 2020Review
- Mutational Analysis of the Structure and Function of the Chaperoning Domain of UNC-45B.Biophysical journal · 2020Article
- Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.Nature communications · 2019Article
- UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins.Nature communications · 2018Article
- UNC-45a promotes myosin folding and stress fiber assembly.The Journal of cell biology · 2017Article
- Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Still Heart Encodes a Structural HMT, SMYD1b, with Chaperone-Like Function during Fast Muscle Sarcomere Assembly.PloS one · 2015Article
- Getting folded: chaperone proteins in muscle development, maintenance and disease.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.Biophysical journal · 2014Article
- The UNC-45 myosin chaperone: from worms to flies to vertebrates.International review of cell and molecular biology · 2014Review
- Article
- UCS protein Rng3p is essential for myosin-II motor activity during cytokinesis in fission yeast.PloS one · 2013Article
- Expression of the inclusion body myopathy 3 mutation in Drosophila depresses myosin function and stability and recapitulates muscle inclusions and weakness.Molecular biology of the cell · 2012Article
- At the Start of the Sarcomere: A Previously Unrecognized Role for Myosin Chaperones and Associated Proteins during Early Myofibrillogenesis.Biochemistry research international · 2012Article
- X-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.Structure (London, England : 1993) · 2011Article
- Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.Journal of cell science · 2011Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
UNC-45 belongs to the UCS (UNC-45, CRO1, She4p) domain protein family, whose members interact with various classes of myosin. Here we provide structural and biochemical evidence that Escherichia coli-expressed Drosophila UNC-45 (DUNC-45) maintains the integrity of several substrates during heat-induced stress in vitro. DUNC-45 displays chaperone function in suppressing aggregation of the muscle myosin heavy meromyosin fragment, the myosin S-1 motor domain, alpha-lactalbumin and citrate synthase. Biochemical evidence is supported by electron microscopy, which reveals the first structural evidence that DUNC-45 prevents inter- or intra-molecular aggregates of skeletal muscle heavy meromyosin caused by elevated temperatures. We also demonstrate for the first time that UNC-45 is able to refold a denatured substrate, urea-unfolded citrate synthase. Overall, this in vitro study provides insight into the fate of muscle myosin under stress conditions and suggests that UNC-45 protects and maintains the contractile machinery during in vivo stress.
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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.