ArticleThe Journal of cell biology1996
Dictyostelium myosin heavy chain kinase A regulates myosin localization during growth and development.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 70 citations in OpenAlex.
- Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation.Scientific reports · 2016Article
- TRPM7, the cytoskeleton and neuronal death.Channels (Austin, Tex.) · 2013Review
- Myosin heavy chain kinases play essential roles in Ca2+, but not cAMP, chemotaxis and the natural aggregation of Dictyostelium discoideum.Journal of cell science · 2012Article
- Role of B regulatory subunits of protein phosphatase type 2A in myosin II assembly control in Dictyostelium discoideum.Eukaryotic 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
- 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
- Conformational preference of ChaK1 binding peptides: a molecular dynamics study.PMC biophysics · 2010Article
- How a cell crawls and the role of cortical myosin II.Eukaryotic cell · 2009Article
- The effects of extracellular calcium on motility, pseudopod and uropod formation, chemotaxis, and the cortical localization of myosin II in Dictyostelium discoideum.Cell motility and the cytoskeleton · 2009Article
- Linking Ras to myosin function: RasGEF Q, a Dictyostelium exchange factor for RasB, affects myosin II functions.The Journal of cell biology · 2008Article
- Myosin heavy-chain kinase A from Dictyostelium possesses a novel actin-binding domain that cross-links actin filaments.The Biochemical journal · 2006Article
- TRPM7, a novel regulator of actomyosin contractility and cell adhesion.The EMBO journal · 2006Article
- Multiple myosin II heavy chain kinases: roles in filament assembly control and proper cytokinesis in Dictyostelium.Molecular biology of the cell · 2005Article
- Identification and characterization of a novel alpha-kinase with a von Willebrand factor A-like motif localized to the contractile vacuole and Golgi complex in Dictyostelium discoideum.Molecular biology of the cell · 2005Article
- The identification of pats1, a novel gene locus required for cytokinesis in Dictyostelium discoideum.Molecular biology of the cell · 2003Article
- Novel myosin heavy chain kinase involved in disassembly of myosin II filaments and efficient cleavage in mitotic dictyostelium cells.Molecular biology of the cell · 2002Article
- Signaling pathways regulating Dictyostelium myosin II.Journal of muscle research and cell motility · 2002Review
- Localization of fission yeast type II myosin, Myo2, to the cytokinetic actin ring is regulated by phosphorylation of a C-terminal coiled-coil domain and requires a functional septation initiation network.Molecular biology of the cell · 2001Article
- Myosin II dynamics and cortical flow during contractile ring formation in Dictyostelium cells.The Journal of cell biology · 2001Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation of the Dictyostelium myosin II heavy chain (MHC) has a key role in regulating myosin localization in vivo and drives filament disassembly in vitro. Previous molecular analysis of the Dictyostelium myosin II heavy chain kinase (MHCK A) gene has demonstrated that the catalytic domain of this enzyme is extremely novel, showing no significant similarity to the known classes of protein kinases (Futey, L. M., Q. G. Medley, G. P. Côté, and T. T. Egelhoff. 1995. J. Biol. Chem. 270:523-529). To address the physiological roles of this enzyme, we have analyzed the cellular consequences of MHCK A gene disruption (mhck A- cells) and MHCK A overexpression (MHCK A++ cells). The mhck A- cells are viable and competent for tested myosin-based contractile events, but display partial defects in myosin localization. Both growth phase and developed mhck A- cells show substantially reduced MHC kinase activity in crude lysates, as well as significant overassembly of myosin into the Triton-resistant cytoskeletal fractions. MHCK A++ cells display elevated levels of MHC kinase activity in crude extracts, and show reduced assembly of myosin into Triton-resistant cytoskeletal fractions. MHCK A++ cells show reduced growth rates in suspension, becoming large and multinucleated, and arrest at the mound stage during development. These results demonstrate that MHCK A functions in vivo as a protein kinase with physiological roles in regulating myosin II localization and assembly in Dictyostelium cells during both growth and developmental stages.
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