FAM134B-RHD protein clustering drives spontaneous budding of asymmetric membranes
- Living cells constantly remodel the shape of their lipid membranes. In the endoplasmic reticulum (ER), the reticulon homology domain (RHD) of the reticulophagy regulator 1 (RETR1/FAM134B) forms dense autophagic puncta that are associated with membrane removal by ER-phagy. In molecular dynamics (MD) simulations, we find that FAM134B-RHD spontaneously forms clusters, driven in part by curvature-mediated attractions. At a critical size, as in a nucleation process, the FAM134B-RHD clusters induce the formation of membrane buds. The kinetics of budding depends sensitively on protein concentration and bilayer asymmetry. Our MD simulations shed light on the role of FAM134B-RHD in ER-phagy and show that membrane asymmetry can be used to modulate the kinetic barrier for membrane remodeling.
Author: | Marc SiggelORCiDGND, Ramachandra M. BhaskaraORCiD, Melanie K. MoesserORCiD, Ivan ĐikićORCiDGND, Gerhard HummerORCiD |
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URN: | urn:nbn:de:hebis:30:3-734398 |
DOI: | https://doi.org/10.1021/acs.jpclett.1c00031 |
ISSN: | 1948-7185 |
Parent Title (English): | The journal of physical chemistry letters |
Publisher: | American Chemical Society |
Place of publication: | Washington, DC |
Document Type: | Article |
Language: | English |
Year of Completion: | 2021 |
Year of first Publication: | 2021 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Release Date: | 2023/03/27 |
Volume: | 12 |
Issue: | 7 |
Page Number: | 6 |
First Page: | 1926 |
Last Page: | 1931 |
HeBIS-PPN: | 50898081X |
Institutes: | Physik |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Sammlungen: | Universitätspublikationen |
Licence (German): | Creative Commons - CC BY - Namensnennung 4.0 International |