ArticlePLoS biology2004
Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod.
Article in PLoS biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed.
- The RNA-binding protein RNP1A is essential and interacts with contractility kit proteins to facilitate cell mechanics.Journal of cell science · 2026Article
- SuggestingCells · 2024Article
- Particle-based model of mechanosensory contractility kit assembly.Biophysical journal · 2022Article
- 14-3-3 proteins tune non-muscle myosin II assembly.The Journal of biological chemistry · 2018Article
- Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Determinants of myosin II cortical localization during cytokinesis.Current biology : CB · 2010Article
- The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly.The Journal of biological chemistry · 2010Article
- Mechanosensing through cooperative interactions between myosin II and the actin crosslinker cortexillin I.Current biology : CB · 2009Article
- Myosin II tailpiece determines its paracrystal structure, filament assembly properties, and cellular localization.The Journal of biological chemistry · 2009Article
- TRPM7 regulates myosin IIA filament stability and protein localization by heavy chain phosphorylation.Journal of molecular biology · 2008Article
- Reversal of cell polarity and actin-myosin cytoskeleton reorganization under mechanical and chemical stimulation.Biophysical journal · 2008Article
- MHC-IIB filament assembly and cellular localization are governed by the rod net charge.PloS one · 2008Article
- Temperature dependence of myosin-II tail fragment assembly.Journal of muscle research and cell motility · 2008Article
- Characterization of the minimum domain required for targeting budding yeast myosin II to the site of cell division.BMC biology · 2006Article
- TRPM7, a novel regulator of actomyosin contractility and cell adhesion.The EMBO journal · 2006Article
- Distinct pathways control recruitment and maintenance of myosin II at the cleavage furrow during cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors.
Funding
Abstract
Myosin-II thick filament formation in Dictyostelium is an excellent system for investigating the phenomenon of self-assembly, as the myosin molecule itself contains all the information required to form a structure of defined size. Phosphorylation of only three threonine residues can dramatically change the assembly state of myosin-II. We show here that the C-terminal 68 kDa of the myosin-II tail (termed AD-Cterm) assembles in a regulated manner similar to full-length myosin-II and forms bipolar thick filament (BTF) structures when a green fluorescent protein (GFP) "head" is added to the N terminus. The localization of this GFP-AD-Cterm to the cleavage furrow of dividing Dictyostelium cells depends on assembly state, similar to full-length myosin-II. This tail fragment therefore represents a good model system for the regulated formation and localization of BTFs. By reducing regulated BTF assembly to a more manageable model system, we were able to explore determinants of myosin-II self-assembly. Our data support a model in which a globular head limits the size of a BTF, and the large-scale charge character of the AD-Cterm region is important for BTF formation. Truncation analysis of AD-Cterm tail fragments shows that assembly is delicately balanced, resulting in assembled myosin-II molecules that are poised to disassemble due to the phosphorylation of only three threonines.
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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.