ArticleMolecular biology of the cell2005
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.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- Calmodulin-mediated events during the life cycle of the amoebozoan Dictyostelium discoideum.Biological reviews of the Cambridge Philosophical Society · 2020Review
- Calmodulin and Calmodulin Binding Proteins inInternational journal of molecular sciences · 2020Review
- Revisiting Drug Development Against the Neglected Tropical Disease, Amebiasis.Frontiers in cellular and infection microbiology · 2020Review
- Dictyostelium discoideum RabS and Rab2 colocalize with the Golgi and contractile vacuole system and regulate osmoregulation.Journal of biosciences · 2016Article
- Life without double-headed non-muscle myosin II motor proteins.Frontiers in chemistry · 2014Review
- Cell-scale dynamic recycling and cortical flow of the actin-myosin cytoskeleton for rapid cell migration.Biology open · 2013Article
- New insights into roles of acidocalcisomes and contractile vacuole complex in osmoregulation in protists.International review of cell and molecular biology · 2013Review
- A proteomic study of myosin II motor proteins during tumor cell migration.Journal of molecular biology · 2011Article
- 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
- WD repeat domain of Dictyostelium myosin heavy chain kinase C functions in both substrate targeting and cellular localization.Eukaryotic cell · 2010Article
- Roles of an unconventional protein kinase and myosin II in amoeba osmotic shock responses.Traffic (Copenhagen, Denmark) · 2009Article
- Invited Lectures : Overviews Purinergic signalling: past, present and future.Purinergic signalling · 2006Article
- The dictyostelium kinome--analysis of the protein kinases from a simple model organism.PLoS genetics · 2006Article
- Multiple myosin II heavy chain kinases: roles in filament assembly control and proper cytokinesis in Dictyostelium.Molecular biology of the cell · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have identified a new protein kinase in Dictyostelium discoideum that carries the same conserved class of "alpha-kinase" catalytic domain as reported previously in myosin heavy chain kinases (MHCKs) in this amoeba but that has a completely novel domain organization. The protein contains an N-terminal von Willebrand factor A (vWFA)-like motif and is therefore named VwkA. Manipulation of VwkA expression level via high copy number plasmids (VwkA++ cells) or gene disruption (vwkA null cells) results in an array of cellular defects, including impaired growth and multinucleation in suspension culture, impaired development, and alterations in myosin II abundance and assembly. Despite sequence similarity to MHCKs, the purified protein failed to phosphorylate myosin II in vitro. Autophosphorylation activity, however, was enhanced by calcium/calmodulin, and the enzyme can be precipitated from cellular lysates with calmodulin-agarose, suggesting that VwkA may directly bind calmodulin. VwkA is cytosolic in distribution but enriched on the membranes of the contractile vacuole and Golgi-like structures in the cell. We propose that VwkA likely acts indirectly to influence myosin II abundance and assembly behavior and possibly has broader roles than previously characterized alpha kinases in this organism, which all seem to be MHCKs.
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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.