ArticleProceedings of the National Academy of Sciences of the United States of America2010
UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 49 citations in OpenAlex.
- UNC-45 assisted myosin folding depends on a conserved FXNature communications · 2024Article
- The Ovary-Brain Connection.Cells · 2024Article
- UCS Chaperone Folding of the Myosin Head: A Function That Evolved before Animals and Fungi Diverged from a Common Ancestor More than a Billion Years Ago.Biomolecules · 2022Review
- Article
- UNC-45A breaks the microtubule lattice independently of its effects on non-muscle myosin II.Journal of cell science · 2021Article
- Mutational Analysis of the Structure and Function of the Chaperoning Domain of UNC-45B.Biophysical journal · 2020Article
- Molecular regulation of the plasma membrane-proximal cellular steps involved in NK cell cytolytic function.Journal of cell science · 2020Review
- Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin.Nature communications · 2019Article
- The co-chaperone UNC45A is essential for the expression of mitotic kinase NEK7 and tumorigenesis.The Journal of biological chemistry · 2019Article
- UNC-45A Is a Novel Microtubule-Associated Protein and Regulator of Paclitaxel Sensitivity in Ovarian Cancer Cells.Molecular cancer research : MCR · 2019Article
- UCS protein function is partially restored in the Saccharomyces cerevisiae she4 mutant with expression of the human UNC45-GC, but not UNC45-SM.Cell stress & chaperones · 2018Article
- UNC-45A is required for neurite extension via controlling NMII activation.Molecular biology of the cell · 2017Article
- Mutation of the Ser18 phosphorylation site on the sole Saccharomyces cerevisiae UCS protein, She4, can compromise high-temperature survival.Cell stress & chaperones · 2017Article
- Cloning, molecular characterization, and expression analysis of the unc45 myosin chaperone b(unc45b)gene of grass carp (Ctenopharyngodon idellus).Journal of muscle research and cell motility · 2016Article
- UNC-45A Is a Nonmuscle Myosin IIA Chaperone Required for NK Cell Cytotoxicity via Control of Lytic Granule Secretion.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- The myosin chaperone UNC45B is involved in lens development and autosomal dominant juvenile cataract.European journal of human genetics : EJHG · 2014Article
- A Toxoplasma gondii class XIV myosin, expressed in Sf9 cells with a parasite co-chaperone, requires two light chains for fast motility.The Journal of biological chemistry · 2014Article
- Chaperone-enhanced purification of unconventional myosin 15, a molecular motor specialized for stereocilia protein trafficking.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- UNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.Biophysical journal · 2014Article
- Myosin chaperones.Current opinion in structural biology · 2014Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
UNC-45/CRO1/She4p (UCS) proteins have variously been proposed to affect the folding, stability, and ATPase activity of myosins. They are the only proteins known to interact directly with the motor domain. To gain more insight into UCS function, we determined the atomic structure of the yeast UCS protein, She4p, at 2.9 Å resolution. We found that 16 helical repeats are organized into an L-shaped superhelix with an amphipathic N-terminal helix dangling off the short arm of the L-shaped molecule. In the crystal, She4p forms a 193-Å-long, zigzag-shaped dimer through three distinct and evolutionary conserved interfaces. We have identified She4p's C-terminal region as a ligand for a 27-residue-long epitope on the myosin motor domain. Remarkably, this region consists of two adjacent, but distinct, binding epitopes localized at the nucleotide-responsive cleft between the nucleotide- and actin-filament-binding sites. One epitope is situated inside the cleft, the other outside the cleft. After ATP hydrolysis and Pi ejection, the cleft narrows at its base from 20 to 12 Å thereby occluding the inside the cleft epitope, while leaving the adjacent, outside the cleft binding epitope accessible to UCS binding. Hence, one cycle of higher and lower binding affinity would accompany one ATP hydrolysis cycle and a single step in the walk on an actin filament rope. We propose that a UCS dimer links two myosins at their motor domains and thereby functions as one of the determinants for step size of myosin on actin filaments.
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