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FAM134B-RHD Protein Clustering Drives Spontaneous Budding of Asymmetric Membranes.

Authors :
Siggel M
Bhaskara RM
Moesser MK
D Ikić I
Hummer G
Source :
The journal of physical chemistry letters [J Phys Chem Lett] 2021 Feb 25; Vol. 12 (7), pp. 1926-1931. Date of Electronic Publication: 2021 Feb 16.
Publication Year :
2021

Abstract

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.

Details

Language :
English
ISSN :
1948-7185
Volume :
12
Issue :
7
Database :
MEDLINE
Journal :
The journal of physical chemistry letters
Publication Type :
Academic Journal
Accession number :
33591770
Full Text :
https://doi.org/10.1021/acs.jpclett.1c00031