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Myosin 1b is an actin depolymerase

delete2019-11-15
delete15
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OA
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J
Julien Pernier
R
Rémy Kusters
H
Hugo Bousquet
T
Thibaut J. Lagny
A
Antoine Morchain
J
Jean‐François Joanny *
P
Patricia Bassereau *
E
Evelyne Coudrier *
DOI:10.1038/s41467-019-13160-ydelete
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Abstract

Abstract

En 中文
The regulation of actin dynamics is essential for various cellular processes. Former evidence suggests a correlation between the function of non-conventional myosin motors and actin dynamics. Here we investigate the contribution of myosin 1b to actin dynamics using sliding motility assays. We observe that sliding on myosin 1b immobilized or bound to a fluid bilayer enhances actin depolymerization at the barbed end, while sliding on myosin II, although 5 times faster, has no effect. This work reveals a non-conventional myosin motor as another type of depolymerase and points to its singular interactions with the actin barbed end.
Keywords:
DEPOLYMERIZATION
DYNAMICS
MOTORS
FILAMENTS
NETWORK
DEPENDS
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Journal

Nature Communications cover
Nature Communications
IF:
15.7
Papers:
9.2W
Citations:
91.2W

Organization

C
centre national de la recherche scientifique (cnrs)
Scholars:
24.5W
Papers: 18.2W
Citations: 279
C
cnrs - institute of chemistry (inc)
Scholars:
1.7W
Papers: 1.3W
Citations: 19