TY  - JOUR
A1  - Siggel, Marc
A1  - Bhaskara, Ramachandra M.
A1  - Moesser, Melanie K.
A1  - Đikić, Ivan
A1  - Hummer, Gerhard
T1  - FAM134B-RHD protein clustering drives spontaneous budding of asymmetric membranes
T2  - The journal of physical chemistry letters
N2  - 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.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/73439
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-734398
SN  - 1948-7185
VL  - 12
IS  - 7
SP  - 1926
EP  - 1931
PB  - American Chemical Society
CY  - Washington, DC
ER  -