Type-I myosins promote actin polymerization to drive membrane bending in endocytosis.
S. cerevisiae
actin
cell biology
endocytosis
myosin
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
06 08 2019
06 08 2019
Historique:
received:
07
12
2018
accepted:
23
07
2019
entrez:
7
8
2019
pubmed:
7
8
2019
medline:
6
2
2020
Statut:
epublish
Résumé
Clathrin-mediated endocytosis in budding yeast requires the formation of a dynamic actin network that produces the force to invaginate the plasma membrane against the intracellular turgor pressure. The type-I myosins Myo3 and Myo5 are important for endocytic membrane reshaping, but mechanistic details of their function remain scarce. Here, we studied the function of Myo3 and Myo5 during endocytosis using quantitative live-cell imaging and genetic perturbations. We show that the type-I myosins promote, in a dose-dependent way, the growth and expansion of the actin network, which controls the speed of membrane and coat internalization. We found that this myosin-activity is independent of the actin nucleation promoting activity of myosins, and cannot be compensated for by increasing actin nucleation. Our results suggest a new mechanism for type-I myosins to produce force by promoting actin filament polymerization.
Identifiants
pubmed: 31385806
doi: 10.7554/eLife.44215
pii: 44215
pmc: PMC6684269
doi:
pii:
Substances chimiques
Actins
0
MYO3 protein, S cerevisiae
0
MYO5 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
Myosin Type I
EC 3.6.1.-
Myosin Heavy Chains
EC 3.6.4.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Swiss National Science Foundation
ID : 31003A_163267
Pays : Switzerland
Organisme : European Research Council
ID : ERC CoG-724489
Pays : International
Informations de copyright
© 2019, Manenschijn et al.
Déclaration de conflit d'intérêts
HM, AP, MM, AR, JR, MK No competing interests declared
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