ArticleThe Biochemical journal2006
Myosin heavy-chain kinase A from Dictyostelium possesses a novel actin-binding domain that cross-links actin filaments.
Article in The Biochemical journal, 2006. 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, 16 citations in OpenAlex.
- Immunogens in Balamuthia mandrillaris: a proteomic exploration.Parasitology research · 2024Article
- PakB binds to the SH3 domain of Dictyostelium Abp1 and regulates its effects on cell polarity and early development.Molecular biology of the cell · 2013Article
- Dictyostelium huntingtin controls chemotaxis and cytokinesis through the regulation of myosin II phosphorylation.Molecular biology of the cell · 2011Article
- Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the alpha-kinase domain.The Journal of biological chemistry · 2011Article
- Identification of a new mechanism for targeting myosin II heavy chain phosphorylation by Dictyostelium myosin heavy chain kinase B.BMC research notes · 2010Article
- Crystal structure of the alpha-kinase domain of Dictyostelium myosin heavy chain kinase A.Science signaling · 2010Article
- The alpha-kinase family: an exceptional branch on the protein kinase tree.Cellular and molecular life sciences : CMLS · 2010Review
- WD repeat domain of Dictyostelium myosin heavy chain kinase C functions in both substrate targeting and cellular localization.Eukaryotic cell · 2010Article
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5 authors at 1 institution in 1 country.
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Abstract
Myosin heavy-chain kinase A (MHCK A) catalyses the disassembly of myosin II filaments in Dictyostelium cells via myosin II heavy-chain phosphorylation. MHCK A possesses a 'coiled-coil'-enriched domain that mediates the oligomerization, cellular localization and actin-binding activities of the kinase. F-actin (filamentous actin) binding by the coiled-coil domain leads to a 40-fold increase in MHCK A activity. In the present study we examined the actin-binding characteristics of the coiled-coil domain as a means of identifying mechanisms by which MHCK A-mediated disassembly of myosin II filaments can be regulated in the cell. Co-sedimentation assays revealed that the coiled-coil domain of MHCK A binds co-operatively to F-actin with an apparent K(D) of approx. 0.5 muM and a stoichiometry of approx. 5:1 [actin/C(1-498)]. Further analyses indicate that the coiled-coil domain binds along the length of the actin filament and possesses at least two actin-binding regions. Quite surprisingly, we found that the coiled-coil domain cross-links actin filaments into bundles, indicating that MHCK A can affect the cytoskeleton in two important ways: (1) by driving myosin II-filament disassembly via myosin II heavy-chain phosphorylation, and (2) by cross-linking/bundling actin filaments. This discovery, along with other supporting data, suggests a model in which MHCK A-mediated bundling of actin filaments plays a central role in the recruitment and activation of the kinase at specific sites in the cell. Ultimately this provides a means for achieving the robust and highly localized disruption of myosin II filaments that facilitates polarized changes in cell shape during processes such as chemotaxis, cytokinesis and multicellular development.
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