ArticleMolecular biology of the cell2015
Twitchin kinase interacts with MAPKAP kinase 2 in Caenorhabditis elegans striated muscle.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Worm orthologues of cytokinesis-associated proteins CIT and ASPM regulate neuronal microtubule dynamics and polarity in C. elegans.PLoS genetics · 2026Article
- Importance of clitellar tissue in the regeneration ability of earthworm Eudrilus eugeniae.Functional & integrative genomics · 2022Article
- Exploration of the regulatory mechanisms of regeneration, anti-oxidation, anti-aging and the immune response at the post-molt stage ofFrontiers in physiology · 2022Article
- Conformational changes in twitchin kinase in vivo revealed by FRET imaging of freely movingeLife · 2021Article
- Investigating the correlation of muscle function tests and sarcomere organization in C. elegans.Skeletal muscle · 2021Article
- NemaFlex: a microfluidics-based technology for standardized measurement of muscular strength of C. elegans.Lab on a chip · 2018Article
- Twitchin kinase inhibits muscle activity.Molecular biology of the cell · 2017Article
- Muscle contraction phenotypic analysis enabled by optogenetics reveals functional relationships of sarcomere components in Caenorhabditis elegans.Scientific reports · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In Caenorhabditis elegans, twitchin is a giant polypeptide located in muscle A-bands. The protein kinase of twitchin is autoinhibited by 45 residues upstream (NL) and 60 residues downstream (CRD) of the kinase catalytic core. Molecular dynamics simulation on a twitchin fragment revealed that the NL is released by pulling force. However, it is unclear how the CRD is removed. To identify proteins that may remove the CRD, we performed a yeast two-hybrid screen using twitchin kinase as bait. One interactor is MAK-1, C. elegans orthologue of MAPKAP kinase 2. MAPKAP kinase 2 is phosphorylated and activated by p38 MAP kinase. We demonstrate that the CRD of twitchin is important for binding to MAK-1. mak-1 is expressed in nematode body wall muscle, and antibodies to MAK-1 localize between and around Z-disk analogues and to the edge of A-bands. Whereas unc-22 mutants are completely resistant, mak-1 mutants are partially resistant to nicotine. MAK-1 can phosphorylate twitchin NL-Kin-CRD in vitro. Genetic data suggest the involvement of two other mak-1 paralogues and two orthologues of p38 MAP kinase. These results suggest that MAK-1 is an activator of twitchin kinase and that the p38 MAP kinase pathway may be involved in the regulation of twitchin.
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