ArticleThe Journal of cell biology1992
Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 84 citations in OpenAlex.
- Role of the nonhelical tailpiece of myosin-II in regulating filament architecture and function.The Journal of cell biology · 2026Article
- Pregnancy in May-Hegglin Anomaly: Diagnostic Challenges and Management Considerations.Case reports in hematology · 2025Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
- Differential expression of myosin heavy chain isoforms in cardiac segments of gnathostome vertebrates and its evolutionary implications.Frontiers in zoology · 2019Article
- Ordering of myosin II filaments driven by mechanical forces: experiments and theory.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Non-muscle myosin II in disease: mechanisms and therapeutic opportunities.Disease models & mechanisms · 2015Review
- Characterization of three full-length human nonmuscle myosin II paralogs.The Journal of biological chemistry · 2013Article
- Effect of estrogen on molecular and functional characteristics of the rodent vaginal muscularis.The journal of sexual medicine · 2013Article
- 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
- The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly.The Journal of biological chemistry · 2010Article
- Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading.PloS one · 2010Article
- Myosin II tailpiece determines its paracrystal structure, filament assembly properties, and cellular localization.The Journal of biological chemistry · 2009Article
- Role of nonmuscle myosin IIB and N-RAP in cell spreading and myofibril assembly in primary mouse cardiomyocytes.Cell motility and the cytoskeleton · 2008Article
- Unregulated smooth-muscle myosin in human intestinal neoplasia.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Two regions of the tail are necessary for the isoform-specific functions of nonmuscle myosin IIB.Molecular biology of the cell · 2007Article
- PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly.Molecular biology of the cell · 2006Article
- Tuning smooth muscle contraction by molecular motors.Journal of molecular medicine (Berlin, Germany) · 2003Review
- Multimerization via its myosin domain facilitates nuclear localization and inhibition of core binding factor (CBF) activities by the CBFbeta-smooth muscle myosin heavy chain myeloid leukemia oncoprotein.Molecular and cellular biology · 2002Article
- The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties.The Journal of cell biology · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A short nonhelical sequence at the COOH-terminus of vertebrate nonmuscle myosin has been shown to enhance myosin filament assembly. We have analyzed the role of this sequence in chicken intestinal epithelial brush border myosin, using protein engineering/site-directed mutagenesis. Clones encoding the rod region of this myosin were isolated and sequenced. They were truncated at various restriction sites and expressed in Escherichia coli, yielding a series of mutant myosin rods with or without the COOH-terminal tailpiece and with serial deletions from their NH2-termini. Deletion of the 35 residue COOH-terminal nonhelical tailpiece was sufficient to increase the critical concentration for myosin rod assembly by 50-fold (at 150 mM NaCl, pH 7.5), whereas NH2-terminal deletions had only minor effects. The only exception was the longest NH2-terminal deletion, which reduced the rod to 119 amino acids and rendered it assembly incompetent. The COOH-terminal tailpiece could be reduced by 15 amino acids and it still efficiently promoted assembly. We also found that the tailpiece promoted assembly of both filaments and segments; assemblies which have different molecular overlaps. Rod fragments carrying the COOH-terminal tailpiece did not promote the assembly of COOH-terminally deleted material when the two were mixed together. The tailpiece sequence thus has profound effects on assembly, yet it is apparently unstructured and can be bisected without affecting its function. Taken together these observations suggest that the nonhelical tailpiece may act sterically to block an otherwise dominant but unproductive molecular interaction in the self assembly process and does not, as has been previously thought, bind to a specific target site(s) on a neighboring molecule.
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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.