ArticleThe Journal of cell biology1990
Expression of Dictyostelium myosin tail segments in Escherichia coli: domains required for assembly and phosphorylation.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 57 citations in OpenAlex.
- Myosin 2 drives actin contractility in fast-crawling species outside of the amorphean lineage.Current biology : CB · 2025Article
- 14-3-3 proteins tune non-muscle myosin II assembly.The Journal of biological chemistry · 2018Article
- Structural and functional insights on the Myosin superfamily.Bioinformatics and biology insights · 2012Article
- Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Temperature dependence of myosin-II tail fragment assembly.Journal of muscle research and cell motility · 2008Article
- Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod.PLoS biology · 2004Article
- Fifty years of contractility research post sliding filament hypothesis.Journal of muscle research and cell motility · 2004Review
- Dictyostelium and Acanthamoeba myosin II assembly domains go to the cleavage furrow of Dictyostelium myosin II-null cells.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties.The Journal of cell biology · 2002Article
- A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.The Journal of cell biology · 1999Article
- Dictyostelium myosin heavy chain kinase A regulates myosin localization during growth and development.The Journal of cell biology · 1996Article
- Single-headed myosin II acts as a dominant negative mutation in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Expression of light meromyosin in Dictyostelium blocks normal myosin II function.The Journal of cell biology · 1995Article
- A novel positive selection for identifying cold-sensitive myosin II mutants in Dictyostelium.Genetics · 1995Article
- In vitro production of enzymatically active myosin heavy chain.Journal of muscle research and cell motility · 1993Article
- A Dictyostelium myosin II lacking a proximal 58-kDa portion of the tail is functional in vitro and in vivo.Molecular biology of the cell · 1992Article
- Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod.The Journal of cell biology · 1992Article
- Spatial and temporal control of nonmuscle myosin localization: identification of a domain that is necessary for myosin filament disassembly in vivo.The Journal of cell biology · 1991Article
- Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions.The Journal of cell biology · 1990Article
- Genetically engineered truncated myosin in Dictyostelium: the carboxyl-terminal regulatory domain is not required for the developmental cycle.Proceedings of the National Academy of Sciences of the United States of America · 1990Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The assembly of myosins into filaments is a property common to all conventional myosins. The ability of myosins to form filaments is conferred by the tail of the large asymmetric molecule. We are studying cloned portions of the Dictyostelium myosin gene expressed in Escherichia coli to investigate functional properties of defined segments of the myosin tail. We have focused on five segments derived from the 68-kD carboxyl-terminus of the myosin tail. These have been expressed and purified to homogeneity from E. coli, and thus the boundaries of each segment within the myosin gene and protein sequence are known. We identified an internal 34-kD segment of the tail, N-LMM-34, which is required and sufficient for assembly. This 287-amino acid domain represents the smallest tail segment purified from any myosin that is capable of forming highly ordered paracrystals characteristic of myosin. Because the assembly of Dictyostelium myosin can be regulated by phosphorylation of the heavy chain, we have studied the in vitro phosphorylation of the expressed tail segments. We have determined which segments are phosphorylated to a high level by a Dictyostelium myosin heavy chain kinase purified from developed cells. While LMM-68, the 68-kD carboxyl terminus of Dictyostelium myosin, or LMM-58, which lacks the 10-kD carboxyl terminus of LMM-68, are phosphorylated to the same extent as purified myosin, subdomains of these segments do not serve as efficient substrates for the kinase. Thus LMM-58 is one minimal substrate for efficient phosphorylation by the myosin heavy chain kinase purified from developed cells. Taken together these results identify two functional domains in Dictyostelium myosin: a 34-kD assembly domain bounded by amino acids 1533-1819 within the myosin sequence and a larger 58-kD phosphorylation domain bounded by amino acids 1533-2034 within the myosin sequence.
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