Opendata, web and dolomites

PHOSPH-UBIQ-IMMUN

Dynamic interplay between phosphorylation and ubiquitination during plant receptor kinase-mediated immunity

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

Project "PHOSPH-UBIQ-IMMUN" data sheet

The following table provides information about the project.

Coordinator
THE SAINSBURY LABORATORY 

Organization address
address: Norwich Research Park, Colney Lane
city: NORWICH
postcode: NR47UH
website: http://www.tsl.ac.uk

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country United Kingdom [UK]
 Project website http://www.tsl.ac.uk/
 Total cost 195˙454 €
 EC max contribution 195˙454 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2016
 Funding Scheme MSCA-IF-EF-CAR
 Starting year 2017
 Duration (year-month-day) from 2017-07-01   to  2019-08-17

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    THE SAINSBURY LABORATORY UK (NORWICH) coordinator 195˙454.00

Map

 Project objective

The first layer of plant immunity is mediated by the recognition of conserved microbial features known as pathogen-associated molecular patterns (PAMPs) by plasma membrane-localized pattern recognition receptors (PRRs). An immediate downstream substrate of activated PRR complexes is the cytoplasmic kinase BIK1, which is a positive regulator of PAMP-triggered immunity (PTI). The objective of this proposal is to uncover how BIK1 regulates plant immune signalling via the characterization of its substrates in PTI. The host laboratory has recently identified a potential BIK1 phosphorylation motif, which is present in 22 Arabidopsis proteins that are rapidly phosphorylated upon PAMP treatment. Eight of these proteins have been confirmed as true BIK1 phosphorylation substrates and include several proteins involved in protein ubiquitination/deubiquitination, including an E3 ubiquitin ligase and two ubiquitin specific proteases (USPs), which will be the focus of this study. Preliminary data indicate that the E3 ubiquitin ligase is a positive regulator of PTI. Here, I will further characterize the role of this E3 ubiquitin ligase in PTI by characterising the role of its phosphorylation by BIK1, and identifying its substrates and their role in PTI using genetic and biochemical approaches. A similar approach will be used to decipher the role of the two USPs in PTI. The project will directly benefit from my previous experience in working with deubiquitinating enzymes during plant development, which will provide all the necessary technical and theoretical knowledge to ensure the project’s success. This exciting project will allow me resuming my career in science, thus corresponding to the objectives of the People Work Programme. At the end of the project, we will have a better understanding on how activated PRR complexes regulate downstream immune signalling, which is a very important question in innate immunity, in both plants and mammals.

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "PHOSPH-UBIQ-IMMUN" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "PHOSPH-UBIQ-IMMUN" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.3.2.)

MIRAGE (2019)

Measuring Interstellar Reactions of Aromatics by Gas-phase Experiments

Read More  

DEAP (2019)

Development of Epithelium Apical Polarity: Does the mechanical cell-cell adhesions play a role?

Read More  

ROAR (2019)

Investigating the Role of Attention in Reading

Read More