PP1TOOLS

Development of chemical biology tools for the elucidation of protein phosphatase-1 substrates and druggability

 Coordinatore EUROPEAN MOLECULAR BIOLOGY LABORATORY 

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 Nazionalità Coordinatore Germany [DE]
 Totale costo 1˙164˙516 €
 EC contributo 1˙164˙516 €
 Programma FP7-IDEAS-ERC
Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call ERC-2013-StG
 Funding Scheme ERC-SG
 Anno di inizio 2014
 Periodo (anno-mese-giorno) 2014-01-01   -   2018-12-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    EUROPEAN MOLECULAR BIOLOGY LABORATORY

 Organization address address: Meyerhofstrasse 1
city: HEIDELBERG
postcode: 69117

contact info
Titolo: Dr.
Nome: Maja
Cognome: Banks-Köhn
Email: send email
Telefono: +49 6221 3878544
Fax: +49 6221 3878575

DE (HEIDELBERG) hostInstitution 1˙164˙516.00
2    EUROPEAN MOLECULAR BIOLOGY LABORATORY

 Organization address address: Meyerhofstrasse 1
city: HEIDELBERG
postcode: 69117

contact info
Titolo: Ms.
Nome: Virginia
Cognome: Otón García
Email: send email
Telefono: 4962210000000
Fax: 4962210000000

DE (HEIDELBERG) hostInstitution 1˙164˙516.00

Mappa


 Word cloud

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selectively    pp    proteins    tools    pstp    holoenzymes    interacting    specificity    protein    kinases    dephosphorylation    counteracting    substrate    selective    phosphatase    cells    activator    chemical   

 Obiettivo del progetto (Objective)

'Protein serine/threonine phosphatases (PSTPs) are considered undruggable although they are involved in the most prominent post-translational modifications. This is mainly due to an apparent lack of substrate specificity. One important PSTP is protein phosphatase-1 (PP1), a ubiquitous PSTP that is predicted to catalyze about 1/3rd of Ser and Thr dephosphorylations in eukaryotic cells, counteracting hundreds of kinases. PP1 has broad substrate specificity but is restrained in vivo by numerous PP1-interacting proteins functioning for example as substrate-targeting proteins and forming specific holoenzymes with PP1. PP1 holoenzymes play a role in many different diseases such as cancer (counteracting oncogenic kinases), diabetes (insulin release), Alzheimer’s (dephosphorylation of Tau protein) and HIV (viral translation). Currently, there are no chemical modulators available that target PP1 selectively, except that we recently developed the first compound that selectively activates PP1 in intact cells, leading to rapid dephosphorylation of PP1 substrates. The activator does not act on the most closely related protein phosphatase-2A. This proposal aims to generate and apply tools for the investigation of PP1, in part based on our previously developed activator. The tools include selective, photo- and enzymatically releasable chemical inhibitors and activators and semisynthetic proteins, and they will be applied to study PP1–substrate interactions and help identify the correlating interacting proteins. The proposed research will provide long-sought selective chemical tools to study PP1 by applying new concepts of activator and inhibitor design using peptide and small molecule chemistry to an enzyme class that is difficult to be targeted chemically. This research program will contribute to a much more detailed understanding of PP1 biology, and will open doors to investigate PP1 and its holoenzymes as drug targets.'

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