Imperial College London
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Dr Tolga Bozkurt

Faculty of Natural Sciences, Department of Life Sciences

Reader in Molecular Plant-Microbe
 
 
 
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Contact

 

+44 (0)20 7594 5381o.bozkurt

 
 
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Location

 

6167Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Zess:2019:10.1371/journal.pbio.3000373,
author = {Zess, EK and Jensen, C and Cruz-Mireles, N and De, la Concepcion JC and Sklenar, J and Stephani, M and Imre, R and Roitinger, E and Hughes, R and Belhaj, K and Mechtler, K and Menke, FLH and Bozkurt, T and Banfield, MJ and Kamoun, S and Maqbool, A and Dagdas, YF},
doi = {10.1371/journal.pbio.3000373},
journal = {PLoS Biology},
pages = {1--27},
title = {N-terminal beta-strand underpins biochemical specialization of an ATG8 isoform},
url = {http://dx.doi.org/10.1371/journal.pbio.3000373},
volume = {17},
year = {2019}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Autophagy-related protein 8 (ATG8) is a highly conserved ubiquitin-like protein that modulates autophagy pathways by binding autophagic membranes and a number of proteins, including cargo receptors and core autophagy components. Throughout plant evolution, ATG8 has expanded from a single protein in algae to multiple isoforms in higher plants. However, the degree to which ATG8 isoforms have functionally specialized to bind distinct proteins remains unclear. Here, we describe a comprehensive protein–protein interaction resource, obtained using in planta immunoprecipitation (IP) followed by mass spectrometry (MS), to define the potato ATG8 interactome. We discovered that ATG8 isoforms bind distinct sets of plant proteins with varying degrees of overlap. This prompted us to define the biochemical basis of ATG8 specialization by comparing two potato ATG8 isoforms using both in vivo protein interaction assays and in vitro quantitative binding affinity analyses. These experiments revealed that the N-terminal β-strand—and, in particular, a single amino acid polymorphism—underpins binding specificity to the substrate PexRD54 by shaping the hydrophobic pocket that accommodates this protein’s ATG8-interacting motif (AIM). Additional proteomics experiments indicated that the N-terminal β-strand shapes the broader ATG8 interactor profiles, defining interaction specificity with about 80 plant proteins. Our findings are consistent with the view that ATG8 isoforms comprise a layer of specificity in the regulation of selective autophagy pathways in plants.
AU  - Zess,EK
AU  - Jensen,C
AU  - Cruz-Mireles,N
AU  - De,la Concepcion JC
AU  - Sklenar,J
AU  - Stephani,M
AU  - Imre,R
AU  - Roitinger,E
AU  - Hughes,R
AU  - Belhaj,K
AU  - Mechtler,K
AU  - Menke,FLH
AU  - Bozkurt,T
AU  - Banfield,MJ
AU  - Kamoun,S
AU  - Maqbool,A
AU  - Dagdas,YF
DO  - 10.1371/journal.pbio.3000373
EP  - 27
PY  - 2019///
SN  - 1544-9173
SP  - 1
TI  - N-terminal beta-strand underpins biochemical specialization of an ATG8 isoform
T2  - PLoS Biology
UR  - http://dx.doi.org/10.1371/journal.pbio.3000373
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000478922100023&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - https://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.3000373
UR  - http://hdl.handle.net/10044/1/90281
VL  - 17
ER  -
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