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Lysine acetylation regulates the interaction between proteins and membranes

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Item Type:Article
Title:Lysine acetylation regulates the interaction between proteins and membranes
Creators Name:Okada, A.K. and Teranishi, K. and Ambroso, M.R. and Isas, J.M. and Vazquez-Sarandeses, E. and Lee, J.Y. and Melo, A.A. and Pandey, P. and Merken, D. and Berndt, L. and Lammers, M. and Daumke, O. and Chang, K. and Haworth, I.S. and Langen, R.
Abstract:Lysine acetylation regulates the function of soluble proteins in vivo, yet it remains largely unexplored whether lysine acetylation regulates membrane protein function. Here, we use bioinformatics, biophysical analysis of recombinant proteins, live-cell fluorescent imaging and genetic manipulation of Drosophila to explore lysine acetylation in peripheral membrane proteins. Analysis of 50 peripheral membrane proteins harboring BAR, PX, C2, or EHD membrane-binding domains reveals that lysine acetylation predominates in membrane-interaction regions. Acetylation and acetylation-mimicking mutations in three test proteins, amphiphysin, EHD2, and synaptotagmin1, strongly reduce membrane binding affinity, attenuate membrane remodeling in vitro and alter subcellular localization. This effect is likely due to the loss of positive charge, which weakens interactions with negatively charged membranes. In Drosophila, acetylation-mimicking mutations of amphiphysin cause severe disruption of T-tubule organization and yield a flightless phenotype. Our data provide mechanistic insights into how lysine acetylation regulates membrane protein function, potentially impacting a plethora of membrane-related processes.
Keywords:Acetylation, Computational Biophysics, Membrane Biophysics, Membrane Curvature, Membrane Lipids, Animals, Drosophila
Source:Nature Communications
ISSN:2041-1723
Publisher:Nature Publishing Group
Volume:12
Number:1
Page Range:6466
Date:9 November 2021
Official Publication:https://doi.org/10.1038/s41467-021-26657-2
PubMed:View item in PubMed

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