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.

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Metadaten
Author:Marc SiggelORCiDGND, Ramachandra M. BhaskaraORCiD, Melanie K. MoesserORCiD, Ivan ĐikićORCiDGND, Gerhard HummerORCiD
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):License LogoCreative Commons - CC BY - Namensnennung 4.0 International