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FAM134B-RHD Protein Clustering Drives Spontaneous Budding of Asymmetric Membranes

MPG-Autoren
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Siggel,  Marc
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Bhaskara,  Ramachandra
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt am Main, Germany;
Buchmann Institute of Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany;

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Moesser,  Melanie K.
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Đikić,  Ivan       
Institute of Biochemistry II, Faculty of Medicine, Goethe University Frankfurt, Frankfurt am Main, Germany;
Buchmann Institute of Molecular Life Sciences, Goethe University Frankfurt, Frankfurt am Main, Germany;
Max Planck Fellow Group ER remodelling Group, Prof. Ivan Đikić, Max Planck Institute of Biophysics, Max Planck Society;

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Hummer,  Gerhard       
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics, Goethe University Frankfurt, Frankfurt am Main, Germany;

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Zitation

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


Zitierlink: https://hdl.handle.net/21.11116/0000-0008-01EB-E
Zusammenfassung
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.