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Development of a tool kit to investigate protein ubiquitylation in biomedical research

Total Cost €


EC-Contrib. €






 UBIQUITON project word cloud

Explore the words cloud of the UBIQUITON project. It provides you a very rough idea of what is the project "UBIQUITON" about.

applicability    cells    neurodegeneration    biotechnology    linkage    diseases    cell    feasibility    proteins    enzymes    human    experimental    complete    biochemical    compartment    tool    appropriate    plays    polyubiquitylated    function    compartments    fundamental    biological    biology    protein    subcellular    ubiquitylation    molecular    cytoplasm    vitro    ubiquiton    appended    membranes    constructs    wishing    cancer    expression    physiology    tags    ubiquitin    polyubiquitylation    biologist    inducible    desired    discovery    inflammation    virtually    tailor    serve    verifying    predominantly    named    interaction    internal    poorly    largely    prepare    disease    versatility    causes    polyubiquitin    mediated    welfare    health    overcome    nucleus    kit    chains    selective    signalling    linkages    made    critical    recombinant    lack    deregulation    types    vivo    innovative    living    demonstrated    induce    manipulation    substrate    fate    establishing    combination   

Project "UBIQUITON" data sheet

The following table provides information about the project.


Organization address
city: MAINZ
postcode: 55128

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 Germany [DE]
 Total cost 149˙900 €
 EC max contribution 149˙900 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2017-PoC
 Funding Scheme ERC-POC
 Starting year 2018
 Duration (year-month-day) from 2018-03-01   to  2019-10-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

Protein ubiquitylation plays a key role in determining the function and fate of proteins in virtually every biological pathway. The deregulation of such fundamental processes causes various diseases, such as cancer, neurodegeneration and inflammation. Understanding the impact of ubiquitylation is therefore critical for improving human health and welfare. Ubiquitin signalling is predominantly mediated by polyubiquitin chains of distinct linkages. Yet, this process is still poorly understood, largely due to a complete lack of methods for the manipulation of ubiquitin linkage. Here we propose to overcome this problem by establishing an inducible system for substrate- and linkage-selective polyubiquitylation of any target protein in vitro or in living cells. This innovative research tool, which we have named the “Ubiquiton” system, is based on a set of recombinant, tailor-made ubiquitylation enzymes in combination with appropriate tags appended to the desired substrate proteins. Having demonstrated feasibility of the method in principle, we now aim at developing the system for general use as a research and discovery tool kit for molecular biology and biotechnology. To this end, we will design expression constructs for a range of experimental systems and subcellular compartments and demonstrate the versatility of the method in different cell types, verifying its applicability in compartment-specific processes in the nucleus, the cytoplasm and at internal membranes. The Ubiquiton system will enable researchers to induce linkage-specific polyubiquitylation of desired targets in vivo and in vitro, prepare polyubiquitylated proteins for biochemical analysis, identify linkage-specific interaction partners and control protein fate in living cells. It will therefore serve as an innovative research tool for any molecular or cell biologist wishing to investigate the physiology of polyubiquitylation in health and disease.


year authors and title journal last update
List of publications.
2019 Renz C, Tröster V, Albert TK, Santt O, Jacobs SC, Khmelinskii A, Ulrich HD
The ubiquitin-conjugating enzyme Ubc13-Mms2 cooperates with a family of FYVE-type-RING ubiquitin protein ligases in K63-polyubiquitylation at internal membranes.
published pages: , ISSN: , DOI: 10.1101/575241

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