ArticleThe Journal of cell biology1989
Intermolecular versus intramolecular interactions of Dictyostelium myosin: possible regulation by heavy chain phosphorylation.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 84 citations in OpenAlex.
- PTEN and the PTEN-like phosphatase CnrN have both distinct and overlapping roles in a Dictyostelium chemorepulsion pathway.Journal of cell science · 2024Article
- SuggestingCells · 2024Article
- Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Various Themes of Myosin Regulation.Journal of molecular biology · 2016Review
- Life without double-headed non-muscle myosin II motor proteins.Frontiers in chemistry · 2014Review
- Regulation of the filament structure and assembly of Acanthamoeba myosin II by phosphorylation of serines in the heavy-chain nonhelical tailpiece.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Regulated offloading of cytoplasmic dynein from microtubule plus ends to the cortex.Developmental cell · 2011Article
- Temperature dependence of myosin-II tail fragment assembly.Journal of muscle research and cell motility · 2008Article
- Protein kinase Cgamma regulates myosin IIB phosphorylation, cellular localization, and filament assembly.Molecular biology of the cell · 2006Article
- Biological, biochemical, and kinetic effects of mutations of the cardiomyopathy loop of Dictyostelium myosin II: importance of ALA400.The Journal of biological chemistry · 2005Article
- Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod.PLoS biology · 2004Article
- Myosin-II reorganization during mitosis is controlled temporally by its dephosphorylation and spatially by Mid1 in fission yeast.The Journal of cell biology · 2004Article
- A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.The Journal of cell biology · 1999Article
- Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Article
- Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells.The Journal of cell biology · 1997Article
- Myosin heavy chain phosphorylation sites regulate myosin localization during cytokinesis in live cells.Molecular biology of the cell · 1997Article
- 14-3-3 inhibits the Dictyostelium myosin II heavy-chain-specific protein kinase C activity by a direct interaction: identification of the 14-3-3 binding domain.Molecular biology of the cell · 1997Article
- Chemoattractant-mediated increases in cGMP induce changes in Dictyostelium myosin II heavy chain-specific protein kinase C activities.The Journal of cell biology · 1996Article
- The role of calcium in aggregation and development of Dictyostelium.Experientia · 1995Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dictyostelium myosin has been examined under conditions that reveal intramolecular and intermolecular interactions that may be important in the process of assembly and its regulation. Rotary shadowed myosin molecules exhibit primarily two configurations under these conditions: straight parallel dimers and folded monomers. All of the monomers bend in a specific region of the 1860-A-long tail that is 1200 A from the head-tail junction. Molecules in parallel dimers are staggered by 140 A, which is a periodicity in the packing of myosin molecules originally observed in native thick filaments of muscle. The most common region for interaction in the dimers is a segment of the tail about 200-A-long, extending from 900 to 1100 A from the head-tail junction. Parallel dimers form tetramers by way of antiparallel interactions in their tail regions with overlaps in multiples of 140 A. The folded configuration of the myosin molecules is promoted by phosphorylation of the heavy chain by Dictyostelium myosin heavy chain kinase. It appears that the bent monomers are excluded from filaments formed upon addition of salt while the dimeric molecules assemble. These results may provide the structural basis for primary steps in myosin filament assembly and its regulation by heavy chain phosphorylation.
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Registered trials
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.