ArticleBiophysical journal2012
Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Optogenetic induction of mechanical muscle stress identifies myosin regulatory ubiquitin ligase NHL-1 in C. elegans.Nature communications · 2024Article
- PEGylated Polymeric Nanoparticles Loaded with 2-Methoxyestradiol for the Treatment of Uterine Leiomyoma in a Patient-Derived Xenograft Mouse Model.Journal of pharmaceutical sciences · 2023Article
- Photophysical Properties of BADAN Revealed in the Study of GGBP Structural Transitions.International journal of molecular sciences · 2021Article
- Maintaining proteostasis under mechanical stress.EMBO reports · 2021Review
- 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
- The central domain of UNC-45 chaperone inhibits the myosin power stroke.FEBS open bio · 2018Article
- YidC assists the stepwise and stochastic folding of membrane proteins.Nature chemical biology · 2016Article
- Impact of holdase chaperones Skp and SurA on the folding of β-barrel outer-membrane proteins.Nature structural & molecular biology · 2015Article
- UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.Biophysical journal · 2014Article
- Unraveling the mysteries of chaperone interactions of the myosin head.Biophysical journal · 2014Article
- The UNC-45 myosin chaperone: from worms to flies to vertebrates.International review of cell and molecular biology · 2014Review
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- UCS protein Rng3p is essential for myosin-II motor activity during cytokinesis in fission yeast.PloS one · 2013Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Myosins are molecular motors that convert chemical energy into mechanical work. Allosterically coupling ATP-binding, hydrolysis, and binding/dissociation to actin filaments requires precise and coordinated structural changes that are achieved by the structurally complex myosin motor domain. UNC-45, a member of the UNC-45/Cro1/She4p family of proteins, acts as a chaperone for myosin and is essential for proper folding and assembly of myosin into muscle thick filaments in vivo. The molecular mechanisms by which UNC-45 interacts with myosin to promote proper folding of the myosin head domain are not known. We have devised a novel approach, to our knowledge, to analyze the interaction of UNC-45 with the myosin motor domain at the single molecule level using atomic force microscopy. By chemically coupling a titin I27 polyprotein to the motor domain of myosin, we introduced a mechanical reporter. In addition, the polyprotein provided a specific attachment point and an unambiguous mechanical fingerprint, facilitating our atomic force microscopy measurements. This approach enabled us to study UNC-45-motor domain interactions. After mechanical unfolding, the motor domain interfered with refolding of the otherwise robust I27 modules, presumably by recruiting them into a misfolded state. In the presence of UNC-45, I27 folding was restored. Our single molecule approach enables the study of UNC-45 chaperone interactions with myosin and their consequences for motor domain folding and misfolding in mechanistic detail.
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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.