FAM134B-RHD Protein Clustering Drives Spontaneous Budding of Asymmetric Membranes

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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.

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Siggel, M., Bhaskara, R. M., Moesser, M. K., Dikić, I., & Hummer, G. (2021). FAM134B-RHD Protein Clustering Drives Spontaneous Budding of Asymmetric Membranes. Journal of Physical Chemistry Letters, 12(7), 1926–1931. https://doi.org/10.1021/acs.jpclett.1c00031

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