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Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings

Lauren E. Grubb, View ORCID ProfilePaul Derbyshire, Katherine Dunning, View ORCID ProfileCyril Zipfel, View ORCID ProfileFrank L.H. Menke, View ORCID ProfileJacqueline Monaghan
doi: https://doi.org/10.1101/2020.09.16.299883
Lauren E. Grubb
1Department of Biology, Queen’s University, Kingston, Canada
2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
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Paul Derbyshire
2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
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Katherine Dunning
1Department of Biology, Queen’s University, Kingston, Canada
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Cyril Zipfel
2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
3Department of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland
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Frank L.H. Menke
2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
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  • ORCID record for Frank L.H. Menke
  • For correspondence: frank.menke@tsl.ac.uk jacqueline.monaghan@queensu.ca
Jacqueline Monaghan
1Department of Biology, Queen’s University, Kingston, Canada
2The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
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  • For correspondence: frank.menke@tsl.ac.uk jacqueline.monaghan@queensu.ca
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Abstract

Protein phosphorylation and ubiquitination are two of the most abundant forms of post-translational modifications in eukaryotes, regulated by thousands of protein kinases, phosphatases, E3 ubiquitin ligases, and ubiquitin proteases. Although previous studies have catalogued several ubiquitinated proteins in plants (Walton et al., 2016), few membrane-localized proteins have been identified. Receptor kinases (RKs) initiate phosphorylation signal relays that regulate plant growth, development, and stress responses. While the regulatory role of phosphorylation on protein kinase function is well-documented (Couto and Zipfel, 2016), considerably less is known about the role of ubiquitination on protein kinase function, even though protein turnover is critical to their signaling competence and cellular homeostasis. Here we describe the large-scale identification of ubiquitination sites on Arabidopsis proteins associated with or integral to the plasma membrane, including over 100 protein kinases.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted September 17, 2020.
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Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings
Lauren E. Grubb, Paul Derbyshire, Katherine Dunning, Cyril Zipfel, Frank L.H. Menke, Jacqueline Monaghan
bioRxiv 2020.09.16.299883; doi: https://doi.org/10.1101/2020.09.16.299883
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Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings
Lauren E. Grubb, Paul Derbyshire, Katherine Dunning, Cyril Zipfel, Frank L.H. Menke, Jacqueline Monaghan
bioRxiv 2020.09.16.299883; doi: https://doi.org/10.1101/2020.09.16.299883

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