ArticleThe Journal of biological chemistry2012
Cloning, expression, and characterization of a novel molecular motor, Leishmania myosin-XXI.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Molecular features of myosin F adapted for driving actin flows in Toxoplasma gondii.Journal of cell science · 2026Article
- Molecular features of Myosin F adapted for driving actin flows inbioRxiv : the preprint server for biology · 2025Article
- Structure and Functions of Actin and Actin-Binding Proteins inPathogens (Basel, Switzerland) · 2025Review
- Binding partners regulate unfolding of myosin VI to activate the molecular motor.The Biochemical journal · 2022Article
- Myosin VI regulates the spatial organisation of mammalian transcription initiation.Nature communications · 2022Article
- The Myosin Family of Mechanoenzymes: From Mechanisms to Therapeutic Approaches.Annual review of biochemistry · 2020Review
- Deciphering the role of UBA-like domains in intraflagellar distribution and functions of myosin XXI in Leishmania.PloS one · 2020Article
- Emerging Functions of Actins and Actin Binding Proteins in Trypanosomatids.Frontiers in cell and developmental biology · 2020Review
- Evolutionary analyses of myosin genes in trypanosomatids show a history of expansion, secondary losses and neofunctionalization.Scientific reports · 2018Article
- Self-organization of actin networks by a monomeric myosin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Calcium can mobilize and activate myosin-VI.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Calcium signaling in trypanosomatid parasites.Cell calcium · 2015Review
- Calmodulin regulates dimerization, motility, and lipid binding of Leishmania myosin XXI.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of the Leishmania parasite contains two classes of myosin. Myosin-XXI, seemingly the only myosin isoform expressed in the protozoan parasite, has been detected in both the promastigote and amastigote stages of the Leishmania life cycle. It has been suggested to perform a variety of functions, including roles in membrane anchorage, but also long-range directed movements of cargo. However, nothing is known about the biochemical or mechanical properties of this motor. Here we designed and expressed various myosin-XXI constructs using a baculovirus expression system. Both full-length (amino acids 1-1051) and minimal motor domain constructs (amino acids 1-800) featured actin-activated ATPase activity. Myosin-XXI was soluble when expressed either with or without calmodulin. In the presence of calcium (pCa 4.1) the full-length motor could bind a single calmodulin at its neck domain (probably amino acids 809-823). Calmodulin binding was required for motility but not for ATPase activity. Once bound, calmodulin remained stably attached independent of calcium concentration (pCa 3-7). In gliding filament assays, myosin-XXI moved actin filaments at ∼15 nm/s, insensitive to both salt (25-1000 mm KCl) and calcium concentrations (pCa 3-7). Calmodulin binding to the neck domain might be involved in regulating the motility of the myosin-XXI motor for its various cellular functions in the different stages of the Leishmania parasite life cycle.
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