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TitleMechanistic insights into actin force generation during vesicle formation from cryo-electron tomography.
Journal, issue, pagesDev Cell, Vol. 57, Issue 9, Page 1132-11145.e5, Year 2022
Publish dateMay 9, 2022
AuthorsDaniel Serwas / Matthew Akamatsu / Amir Moayed / Karthik Vegesna / Ritvik Vasan / Jennifer M Hill / Johannes Schöneberg / Karen M Davies / Padmini Rangamani / David G Drubin /
PubMed AbstractActin assembly provides force for a multitude of cellular processes. Compared to actin-assembly-based force production during cell migration, relatively little is understood about how actin assembly ...Actin assembly provides force for a multitude of cellular processes. Compared to actin-assembly-based force production during cell migration, relatively little is understood about how actin assembly generates pulling forces for vesicle formation. Here, cryo-electron tomography identified actin filament number, organization, and orientation during clathrin-mediated endocytosis in human SK-MEL-2 cells, showing that force generation is robust despite variance in network organization. Actin dynamics simulations incorporating a measured branch angle indicate that sufficient force to drive membrane internalization is generated through polymerization and that assembly is triggered from ∼4 founding "mother" filaments, consistent with tomography data. Hip1R actin filament anchoring points are present along the entire endocytic invagination, where simulations show that it is key to pulling force generation, and along the neck, where it targets filament growth and makes internalization more robust. Actin organization described here allowed direct translation of structure to mechanism with broad implications for other actin-driven processes.
External linksDev Cell / PubMed:35504288 / PubMed Central
MethodsEM (tomography) / EM (subtomogram averaging)
Resolution27.0 Å
Structure data

EMDB-26483: Actin organization during clathrin-mediated endocytosis
Method: EM (tomography)

EMDB-26484: In situ map of the clathrin hub
Method: EM (subtomogram averaging) / Resolution: 27.0 Å

Source
  • Homo sapiens (human)

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