ArticleBiochemistry2006
Temperature dependence of nucleotide association and kinetic characterization of myo1b.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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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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
27 citing papers in PubMed, 36 citations in OpenAlex.
- High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- High resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory.bioRxiv : the preprint server for biology · 2025Article
- Myosin-I synergizes with Arp2/3 complex to enhance the pushing forces of branched actin networks.Science advances · 2024Article
- Myosin-I Synergizes with Arp2/3 Complex to Enhance Pushing Forces of Branched Actin Networks.bioRxiv : the preprint server for biology · 2024Article
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- Endocytic myosin-1 is a force-insensitive, power-generating motor.The Journal of cell biology · 2023Article
- Endocytic myosin-1 is a force-insensitive, power-generating motor.bioRxiv : the preprint server for biology · 2023Article
- Article
- Myosin 1b is an actin depolymerase.Nature communications · 2019Article
- N-terminal splicing extensions of the humanThe Journal of biological chemistry · 2017Article
- ROS induced distribution of mitochondria to filopodia by Myo19 depends on a class specific tryptophan in the motor domain.Scientific reports · 2017Article
- Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips.Scientific reports · 2017Article
- A Perspective on the Role of Myosins as Mechanosensors.Biophysical journal · 2016Article
- Mathematical Characterization of Protein Sequences Using Patterns as Chemical Group Combinations of Amino Acids.PloS one · 2016Article
- Mechanochemical tuning of myosin-I by the N-terminal region.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Myosin IC generates power over a range of loads via a new tension-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Calcium regulation of myosin-I tension sensing.Biophysical journal · 2012Article
- A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myo1b is a widely expressed myosin-I isoform that concentrates on endosomal and ruffling membranes and is thought to play roles in membrane trafficking and dynamics. It is one of the best characterized myosin-I isoforms and appears to have unique biochemical properties tuned for tension sensing or tension maintenance. We determined the key biochemical rate constants that define the actomyo1b ATPase cycle at 37 degrees C and measured the temperature dependence of ATP binding, ADP release, and the transition from a nucleotide-inaccessible state to a nucleotide-accessible state (k(alpha)). The rate of ATP binding is highly temperature sensitive, with an Arrhenius activation energy 2-3-fold greater than other characterized myosins (e.g., myosin-II and myosin-V). ATP hydrolysis is fast, and phosphate release is slow and rate limiting with an actin dependence that is nearly identical to the steady-state ATPase parameters (Vmax and K(ATPase)). ADP release is not as temperature dependent as ATP binding. The rates and temperature dependence of ADP release are similar to k(alpha) suggesting that a similar structural change is responsible for both transitions. We calculate a duty ratio of 0.08 based on the biochemical kinetics. However, this duty ratio is likely to be highly sensitive to strain.
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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.