ArticlePloS one2014
The loop2 insertion of type IX myosin acts as an electrostatic actin tether that permits processive movement.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 19 citations in OpenAlex.
- Myosin IXB protects immune cells from virus infection.The Journal of general virology · 2025Article
- Insights into Actin Isoform-Specific Interactions with Myosin via Computational Analysis.Molecules (Basel, Switzerland) · 2024Article
- Unconventional Myosins fromBiomolecules · 2022Review
- Review
- Myosins, an Underestimated Player in the Infectious Cycle of Pathogenic Bacteria.International journal of molecular sciences · 2021Review
- Squeezing in a Meal: Myosin Functions in Phagocytosis.Trends in cell biology · 2020Review
- Myosins in Osteoclast Formation and Function.Biomolecules · 2018Review
- Self-organization of actin networks by a monomeric myosin.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although class IX myosins are single-headed, they demonstrate characteristics of processive movement along actin filaments. Double-headed myosins that move processively along actin filaments achieve this by successive binding of the two heads in a hand-over-hand mechanism. This mechanism, obviously, cannot operate in single-headed myosins. However, it has been proposed that a long class IX specific insertion in the myosin head domain at loop2 acts as an F-actin tether, allowing for single-headed processive movement. Here, we tested this proposal directly by analysing the movement of deletion constructs of the class IX myosin from Caenorhabditis elegans (Myo IX). Deletion of the large basic loop2 insertion led to a loss of processive behaviour, while deletion of the N-terminal head extension, a second unique domain of class IX myosins, did not influence the motility of Myo IX. The processive behaviour of Myo IX is also abolished with increasing salt concentrations. These observations directly demonstrate that the insertion located in loop2 acts as an electrostatic actin tether during movement of Myo IX along the actin track.
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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.