Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.
catch bond
molecular motor
myosin-V
run length
unbinding rate
Journal
Journal of the Royal Society, Interface
ISSN: 1742-5662
Titre abrégé: J R Soc Interface
Pays: England
ID NLM: 101217269
Informations de publication
Date de publication:
04 2020
04 2020
Historique:
entrez:
8
4
2020
pubmed:
8
4
2020
medline:
22
6
2021
Statut:
ppublish
Résumé
An analytical theory is presented for the dynamics of myosin-V molecular motor, where both ATP-dependent and ATP-independent steppings are taken into account. Specifically, the dependences of velocity, run length and unbinding rate upon both forward and backward loads and ATP concentration are studied, explaining quantitatively the diverse available single-molecule data and providing predicted results. The results show that the unbinding rate increases with the increase of ATP concentration and levels off at both low and high ATP concentrations. More interestingly, at an ATP concentration that is not very low, the unbinding rate exhibits characteristics of a catch-slip bond under backward load, with the unbinding rate decreasing rapidly with the increase of the backward load in the range smaller than about 2.5 pN and then increasing slowly with the further increase of the backward load. By contrast, under forward load the unbinding rate exhibits a slip-bond characteristic.
Identifiants
pubmed: 32259459
doi: 10.1098/rsif.2020.0029
pmc: PMC7211485
doi:
Substances chimiques
Actins
0
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
20200029Références
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