MOBA-CS

The molecular basis of Cockayne Syndrome

Coordinatore	FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	Switzerland [CH]
Totale costo	1˙499˙235 €
EC contributo	1˙499˙235 €
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-2010-StG_20091118
Funding Scheme	ERC-SG
Anno di inizio	2011
Periodo (anno-mese-giorno)	2011-01-01   -   2015-12-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	Novartis Forschungsstiftung  Organization address address: Maulbeerstrasse 66 city: BASEL postcode: 4058 contact info Titolo: Ms. Nome: Dorothy Cognome: Searles Email: send email Telefono: +41 61 6972982 Fax: +41 61 6973976	CH (BASEL)	beneficiary	0.00
2	FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH  Organization address address: MAULBEERSTRASSE 66 city: BASEL postcode: 4058 contact info Titolo: Dr. Nome: Nicolas Cognome: Thomä Email: send email Telefono: +41 61 697 86 30 Fax: +41 61 69739 76	CH (BASEL)	hostInstitution	1˙499˙235.00
3	FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH  Organization address address: MAULBEERSTRASSE 66 city: BASEL postcode: 4058 contact info Titolo: Mrs. Nome: Searles Cognome: Dorothy Email: send email Telefono: +41 61 6972982 Fax: +41 61 6973976	CH (BASEL)	hostInstitution	1˙499˙235.00

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 Obiettivo del progetto (Objective)

'Cockayne syndrome is a congenital disease with impaired DNA repair in actively transcribed genes. Affected children show developmental abnormalities and signs of premature aging. Cockayne syndrome is caused by mutations in the Cockayne syndrome complementation group A (CSA) and B (CSB) genes. While CSB encodes a SWI/SNF ATPase that likely assists the stalled RNA polymerase in overcoming lesions, CSA’s detailed role in repair has so far remained elusive. CSA is part of the DDB1-CSA-Cul4-Rbx1 E3 ubiquitin ligase complex. The available data suggest that CSA may function as a substrate adaptor for ubiquitination by the DDB1-Cul4-Rbx1 ligase. I will pursue a novel structure-driven proteomic approach to identify the substrate epitope recognized by the DDB1-CSA-Cul4-Rbx1 E3 ubiquitin ligase. These experiments aim to provide the important missing signal required for recruitment of the ligase complex to sites of stalled RNA polII complexes. Importantly, the CSA ligase, as it arrives at sites of DNA damage, is inactive. Our comprehensive structural and biochemical efforts will thus include the mechanisms of regulation of the CSA ubiquitin ligase activity by activators and inhibitors following recruitment to the repair site. MoBa-CS will not only improve our understanding of CSA’s molecular role in Cockayne syndrome, but also reveal CSA’s mode of action within the essential transcription coupled repair pathway. Understanding the cellular signals overseeing transcription coupled repair will provide important insights into how the pathway is integrated within the overall DNA damage response circuitry of the cell. ERC funding would enable us to pursue an interdisciplinary proteomic and structure based approach in examining DDB1-CSA function.'