ArticleGenetics2010
Caenorhabditis elegans unc-82 encodes a serine/threonine kinase important for myosin filament organization in muscle during growth.
Article in Genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 38 citations in OpenAlex.
- Trial
- Identification of CryAB as a target of NUAK kinase activity in Drosophila muscle tissue.Genetics · 2023Article
- Independent pathways control muscle tissue size and sarcomere remodeling.Developmental biology · 2022Article
- Investigating the correlation of muscle function tests and sarcomere organization in C. elegans.Skeletal muscle · 2021Article
- Role of ARK5 in cancer and other diseases (Review).Experimental and therapeutic medicine · 2021Review
- Drosophila NUAK functions with Starvin/BAG3 in autophagic protein turnover.PLoS genetics · 2020Article
- Protein phosphatase 2A is crucial for sarcomere organization in Caenorhabditis elegans striated muscle.Molecular biology of the cell · 2018Article
- The SEK-1 p38 MAP Kinase Pathway Modulates Gq Signaling inG3 (Bethesda, Md.) · 2017Article
- The Role of the UNC-82 Protein Kinase in Organizing Myosin Filaments in Striated Muscle ofGenetics · 2017Article
- The AMPK-related kinase SNARK regulates muscle mass and myocyte survival.The Journal of clinical investigation · 2016Article
- The Haemonchus contortus kinome--a resource for fundamental molecular investigations and drug discovery.Parasites & vectors · 2015Article
- The sarcomeric M-region: a molecular command center for diverse cellular processes.BioMed research international · 2015Review
- Muscle-specific knock-out of NUAK family SNF1-like kinase 1 (NUAK1) prevents high fat diet-induced glucose intolerance.The Journal of biological chemistry · 2012Article
- Bending amplitude - a new quantitative assay of C. elegans locomotion: identification of phenotypes for mutants in genes encoding muscle focal adhesion components.Methods (San Diego, Calif.) · 2012Article
- Calpains mediate integrin attachment complex maintenance of adult muscle in Caenorhabditis elegans.PLoS genetics · 2012Article
- Identification and prioritization of NUAK1 and PPP1CC as positional candidate loci for skeletal muscle strength phenotypes.Physiological genomics · 2011Article
- NUAK2: an emerging acral melanoma oncogene.Oncotarget · 2011Review
- Molecular structure of sarcomere-to-membrane attachment at M-Lines in C. elegans muscle.Journal of biomedicine & biotechnology · 2010Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations in the unc-82 locus of Caenorhabditis elegans were previously identified by screening for disrupted muscle cytoskeleton in otherwise apparently normal mutagenized animals. Here we demonstrate that the locus encodes a serine/threonine kinase orthologous to human ARK5/SNARK (NUAK1/NUAK2) and related to the PAR-1 and SNF1/AMP-Activated kinase (AMPK) families. The predicted 1600-amino-acid polypeptide contains an N-terminal catalytic domain and noncomplex repetitive sequence in the remainder of the molecule. Phenotypic analyses indicate that unc-82 is required for maintaining the organization of myosin filaments and internal components of the M-line during cell-shape changes. Mutants exhibit normal patterning of cytoskeletal elements during early embryogenesis. Defects in localization of thick filament and M-line components arise during embryonic elongation and become progressively more severe as development proceeds. The phenotype is independent of contractile activity, consistent with unc-82 mutations preventing proper cytoskeletal reorganization during growth, rather than undermining structural integrity of the M-line. This is the first report establishing a role for the UNC-82/ARK5/SNARK kinases in normal development. We propose that activation of UNC-82 kinase during cell elongation regulates thick filament attachment or growth, perhaps through phosphorylation of myosin and paramyosin. We speculate that regulation of myosin is an ancestral characteristic of kinases in this region of the kinome.
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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.