ArticleThe Journal of biological chemistry2017
Kinetic signatures of myosin-5B, the motor involved in microvillus inclusion disease.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Motor properties of Myosin 5c are modulated by tropomyosin isoforms and inhibited by pentabromopseudilin.Frontiers in physiology · 2024Article
- The dynamics of actin protrusions can be controlled by tip-localized myosin motors.The Journal of biological chemistry · 2024Article
- A mutation in switch I alters the load-dependent kinetics of myosin Va.Nature communications · 2023Article
- Article
- Experimental Studies on the Impact of the Projected Ocean Acidification on Fish Survival, Health, Growth, and Meat Quality; Black Sea Bream (Animals : an open access journal from MDPI · 2021Article
- Roles and regulation of myosin V interaction with cargo.Advances in biological regulation · 2021Review
- Myosin V regulates synaptopodin clustering and localization in the dendrites of hippocampal neurons.Journal of cell science · 2019Article
- F-actin patches associated with glutamatergic synapses control positioning of dendritic lysosomes.The EMBO journal · 2019Article
- Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level.Nature communications · 2018Article
- Affimer proteins for F-actin: novel affinity reagents that label F-actin in live and fixed cells.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin-5B is a ubiquitous molecular motor that transports cargo vesicles of the endomembrane system in intracellular recycling pathways. Myosin-5B malfunction causes the congenital enteropathy microvillus inclusion disease, underlining its importance in cellular homeostasis. Here we describe the interaction of myosin-5B with F-actin, nucleotides, and the pyrazolopyrimidine compound myoVin-1. We show that single-headed myosin-5B is an intermediate duty ratio motor with a kinetic ATPase cycle that is rate-limited by the release of phosphate. The presence of a second head generates strain and gating in the myosin-5B dimer that alters the kinetic signature by reducing the actin-activated ADP release rate to become rate-limiting. This kinetic transition into a high-duty ratio motor is a prerequisite for the proposed transport function of myosin-5B in cellular recycling pathways. Moreover, we show that the small molecule compound myoVin-1 inhibits the enzymatic and functional activity of myosin-5B
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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.