ArticleProceedings of the National Academy of Sciences of the United States of America2010
Control of myosin-I force sensing by alternative splicing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 43 citations in OpenAlex.
- MYO1B in human disease: an actin-based motor linking membrane trafficking to oncogenic signaling, metastasis, and vascular aging.Frontiers in oncology · 2026Review
- Force-insensitive myosin-I enhances endocytosis robustness through actin network-scale collective ratcheting.Molecular biology of the cell · 2025Article
- 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
- 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
- The many roles of myosins in filopodia, microvilli and stereocilia.Current biology : CB · 2021Review
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Ras Post-transcriptionally Enhances a Pre-malignantly Primed EMT to Promote Invasion.iScience · 2018Article
- Measuring the Kinetic and Mechanical Properties of Non-processive Myosins Using Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- MEMLET: An Easy-to-Use Tool for Data Fitting and Model Comparison Using Maximum-Likelihood Estimation.Biophysical journal · 2016Article
- Myosin-I molecular motors at a glance.Journal of cell science · 2016Review
- A Perspective on the Role of Myosins as Mechanosensors.Biophysical journal · 2016Article
- The role of myosin 1c and myosin 1b in surfactant exocytosis.Journal of cell science · 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
- Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- 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
- Motor and tail homology 1 (Th1) domains antagonistically control myosin-1 dynamics.Biophysical journal · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myosin-Is are molecular motors that link cellular membranes to the actin cytoskeleton, where they play roles in mechano-signal transduction and membrane trafficking. Some myosin-Is are proposed to act as force sensors, dynamically modulating their motile properties in response to changes in tension. In this study, we examined force sensing by the widely expressed myosin-I isoform, myo1b, which is alternatively spliced in its light chain binding domain (LCBD), yielding proteins with lever arms of different lengths. We found the actin-detachment kinetics of the splice isoforms to be extraordinarily tension-sensitive, with the magnitude of tension sensitivity to be related to LCBD splicing. Thus, in addition to regulating step-size, motility rates, and myosin activation, the LCBD is a key regulator of force sensing. We also found that myo1b is substantially more tension-sensitive than other myosins with similar length lever arms, indicating that different myosins have different tension-sensitive transitions.
Indexed as
Identifiers
What OpenQuestion holds
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.