ArticleEMBO reports2009
Rng3, a member of the UCS family of myosin co-chaperones, associates with myosin heavy chains cotranslationally.
Article in EMBO reports, 2009. 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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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
14 citing papers in PubMed, 21 citations in OpenAlex.
- 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
- Phosphorylation of the RNA-binding protein Zfs1 modulates sexual differentiation in fission yeast.Journal of cell science · 2017Article
- Systematic analysis of the role of RNA-binding proteins in the regulation of RNA stability.PLoS genetics · 2014Article
- Article
- Myosin chaperones.Current opinion in structural biology · 2014Review
- Article
- UCS protein Rng3p is essential for myosin-II motor activity during cytokinesis in fission yeast.PloS one · 2013Article
- The RNA binding protein Csx1 promotes sexual differentiation in Schizosaccharomyces pombe.PloS one · 2012Article
- Widespread cotranslational formation of protein complexes.PLoS genetics · 2011Article
- Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.Journal of cell science · 2011Article
- Dividing the spoils of growth and the cell cycle: The fission yeast as a model for the study of cytokinesis.Cytoskeleton (Hoboken, N.J.) · 2011Review
- Article
- UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Global coordination of transcriptional control and mRNA decay during cellular differentiation.Molecular systems biology · 2010Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The production of functional myosin heavy chains in many eukaryotic organisms requires the function of proteins containing UCS domains (UNC-45/CRO1/She4), which bind to the myosin head domain and stimulate its folding. UCS proteins are essential for myosin-related functions such as muscle formation, RNA localization and cytokinesis. Here, we show that the Schizosaccharomyces pombe UCS protein Rng3 associates with polysomes, suggesting that UCS proteins might assist myosin folding cotranslationally. To identify Rng3 cotranslational targets systematically, we purified Rng3-associated RNAs and used DNA microarrays to identify the transcripts. Rng3 copurified with only seven transcripts (around 0.1% of S. pombe genes), including all five messenger RNAs encoding myosin heavy chains. These results suggest that every myosin heavy chain in S. pombe is a cotranslational target of Rng3. Furthermore, our data suggest that microarray-based approaches allow the genome-wide identification of cotranslational chaperone targets, and thus pave the way for the dissection of translation-linked chaperone networks.
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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.