Molecular mechanics underlying flat-to-round membrane budding in live secretory cells

Wonchul Shin, Ben Zucker, Nidhi Kundu, Sung Hoon Lee, Bo Shi, Chung Yu Chan, Xiaoli Guo, Jonathan T. Harrison, Jaymie Moore Turechek, Jenny E. Hinshaw (), Michael M. Kozlov () and Ling-Gang Wu ()
Additional contact information
Wonchul Shin: National Institute of Neurological Disorders and Stroke
Ben Zucker: Tel Aviv University
Nidhi Kundu: National Institute of Diabetes and Digestive and Kidney Diseases
Sung Hoon Lee: Chung-Ang University
Bo Shi: National Institute of Neurological Disorders and Stroke
Chung Yu Chan: National Institute of Neurological Disorders and Stroke
Xiaoli Guo: National Institute of Neurological Disorders and Stroke
Jonathan T. Harrison: National Institute of Diabetes and Digestive and Kidney Diseases
Jaymie Moore Turechek: National Institute of Neurological Disorders and Stroke
Jenny E. Hinshaw: National Institute of Diabetes and Digestive and Kidney Diseases
Michael M. Kozlov: Tel Aviv University
Ling-Gang Wu: National Institute of Neurological Disorders and Stroke

Nature Communications, 2022, vol. 13, issue 1, 1-18

Abstract: Abstract Membrane budding entails forces to transform flat membrane into vesicles essential for cell survival. Accumulated studies have identified coat-proteins (e.g., clathrin) as potential budding factors. However, forces mediating many non-coated membrane buddings remain unclear. By visualizing proteins in mediating endocytic budding in live neuroendocrine cells, performing in vitro protein reconstitution and physical modeling, we discovered how non-coated-membrane budding is mediated: actin filaments and dynamin generate a pulling force transforming flat membrane into Λ-shape; subsequently, dynamin helices surround and constrict Λ-profile’s base, transforming Λ- to Ω-profile, and then constrict Ω-profile’s pore, converting Ω-profiles to vesicles. These mechanisms control budding speed, vesicle size and number, generating diverse endocytic modes differing in these parameters. Their impact is widespread beyond secretory cells, as the unexpectedly powerful functions of dynamin and actin, previously thought to mediate fission and overcome tension, respectively, may contribute to many dynamin/actin-dependent non-coated-membrane buddings, coated-membrane buddings, and other membrane remodeling processes.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-022-31286-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31286-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-31286-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().