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Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum
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Brooks, Rhiannon and Dixon, Ann M. (2020) Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum. Biochimica et biophysica acta. Biomembranes, 1862 (3). 183160. doi:10.1016/j.bbamem.2019.183160 ISSN 1879-2642.
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WRAP-Revealing-mechanism-interactions-putative-reticulum-Dixon-2020.pdf - Accepted Version - Requires a PDF viewer. Available under License Creative Commons Attribution Non-commercial No Derivatives 4.0. Download (1454Kb) | Preview |
Official URL: https://doi.org/10.1016/j.bbamem.2019.183160
Abstract
Membrane curvature sensing via helical protein domains, such as those identified in Amphiphysin and ArfGAP1, have been linked to a diverse range of cellular processes. However, these regions can vary significantly between different protein families and thus remain challenging to identify from sequence alone. Greater insight into the protein-lipid interactions that drive this behavior could lead to production of therapeutics that specifically target highly curved membranes. Here we demonstrate the curvature-dependence of membrane binding for an amphipathic helix (APH) in a plant reticulon, namely RTNLB13 from A. thaliana. We utilize solution-state nuclear magnetic resonance spectroscopy to establish the exact location of the APH and map the residues involved in protein-membrane interactions at atomic resolution. We find that the hydrophobic residues making up the membrane binding site are conserved throughout all A. thaliana reticulons. Our results also provide mechanistic insight that leads us to propose that membrane binding by this APH may act as a feedback element, only forming when ER tubules reach a critical size and adding stabilization to these structures without disrupting the bilayer. A shallow hydrophobic binding interface appears to be a feature shared more broadly across helical curvature sensors and would automatically restrict the penetration depth of these structures into the membrane. We also suggest this APH is highly tuned to the composition of the membrane in which it resides, and that this property may be universal in curvature sensors thus rationalizing the variety of mechanisms reported for these functional elements. [Abstract copyright: Copyright © 2019. Published by Elsevier B.V.]
| Item Type: | Journal Article | ||||||||
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| Subjects: | Q Science > QH Natural history > QH301 Biology Q Science > QK Botany |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||
| SWORD Depositor: | Library Publications Router | ||||||||
| Library of Congress Subject Headings (LCSH): | Cell membranes, Plant cell membranes, Membranes (Biology) -- Research, Membrane lipids, Endoplasmic reticulum -- Research, Plant genetics, Nuclear magnetic resonance spectroscopy -- Methodology | ||||||||
| Journal or Publication Title: | Biochimica et biophysica acta. Biomembranes | ||||||||
| Publisher: | Elsevier | ||||||||
| ISSN: | 1879-2642 | ||||||||
| Official Date: | 1 March 2020 | ||||||||
| Dates: |
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| Volume: | 1862 | ||||||||
| Number: | 3 | ||||||||
| Article Number: | 183160 | ||||||||
| DOI: | 10.1016/j.bbamem.2019.183160 | ||||||||
| Status: | Peer Reviewed | ||||||||
| Publication Status: | Published | ||||||||
| Access rights to Published version: | Restricted or Subscription Access | ||||||||
| Date of first compliant deposit: | 15 January 2020 | ||||||||
| Date of first compliant Open Access: | 16 December 2020 | ||||||||
| RIOXX Funder/Project Grant: |
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