ArticleBMC cell biology2002
Differential localization in cells of myosin II heavy chain kinases during cytokinesis and polarized migration.
Article in BMC cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 56 citations in OpenAlex.
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- One must reconstitute the functions of interest from purified proteins.Frontiers in physiology · 2024Review
- MYH9 binds to dNTPs via deoxyribose moiety and plays an important role in DNA synthesis.Oncotarget · 2022Article
- Local pulsatile contractions are an intrinsic property of the myosin 2A motor in the cortical cytoskeleton of adherent cells.Molecular biology of the cell · 2017Article
- Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation.Scientific reports · 2016Article
- Genetic suppression of a phosphomimic myosin II identifies system-level factors that promote myosin II cleavage furrow accumulation.Molecular biology of the cell · 2014Article
- Moving towards a paradigm: common mechanisms of chemotactic signaling in Dictyostelium and mammalian leukocytes.Cellular and molecular life sciences : CMLS · 2014Review
- A Cdc42- and Rac-interactive binding (CRIB) domain mediates functions of coronin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
- Cytokinesis mechanics and mechanosensing.Cytoskeleton (Hoboken, N.J.) · 2012Review
- WAVE2 Protein Complex Coupled to Membrane and Microtubules.Journal of oncology · 2012Article
- 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
- WD repeat domain of Dictyostelium myosin heavy chain kinase C functions in both substrate targeting and cellular localization.Eukaryotic cell · 2010Article
- Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading.PloS one · 2010Article
- Eukaryotic chemotaxis: a network of signaling pathways controls motility, directional sensing, and polarity.Annual review of biophysics · 2010Review
- Roles of an unconventional protein kinase and myosin II in amoeba osmotic shock responses.Traffic (Copenhagen, Denmark) · 2009Article
- Massive autophosphorylation of the Ser/Thr-rich domain controls protein kinase activity of TRPM6 and TRPM7.PloS one · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundCortical myosin-II filaments in Dictyostelium discoideum display enrichment in the posterior of the cell during cell migration, and in the cleavage furrow during cytokinesis. Filament assembly in turn is regulated by phosphorylation in the tail region of the myosin heavy chain (MHC). Early studies have revealed one enzyme, MHCK-A, which participates in filament assembly control, and two other structurally related enzymes, MHCK-B and -C. In this report we evaluate the biochemical properties of MHCK-C, and using fluorescence microscopy in living cells we examine the localization of GFP-labeled MHCK-A, -B, and -C in relation to GFP-myosin-II localization.
resultsBiochemical analysis indicates that MHCK-C can phosphorylate MHC with concomitant disassembly of myosin II filaments. In living cells, GFP-MHCK-A displayed frequent enrichment in the anterior of polarized migrating cells, and in the polar region but not the furrow during cytokinesis. GFP-MHCK-B generally displayed a homogeneous distribution. In migrating cells GFP-MHCK-C displayed posterior enrichment similar to that of myosin II, but did not localize with myosin II to the furrow during the early stage of cytokinesis. At the late stage of cytokinesis, GFP-MHCK-C became strongly enriched in the cleavage furrow, remaining there through completion of division.
conclusionMHCK-A, -B, and -C display distinct cellular localization patterns suggesting different cellular functions and regulation for each MHCK isoform. The strong localization of MHCK-C to the cleavage furrow in the late stages of cell division may reflect a mechanism by which the cell regulates the progressive removal of myosin II as furrowing progresses.
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