MAMMALIAN ERAD

EXPANDING THE KNOWLEDGE ON MAMMALIAN ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION (ERAD)

 Coordinatore EGE UNIVERSITESI 

 Organization address address: EGE UNIVERSITY KAMPUSU
city: IZMIR
postcode: 35040

contact info
Titolo: Prof.
Nome: Aysun
Cognome: Pabuccuoglu
Email: send email
Telefono: +90 532 3667701
Fax: +90 232 3885258

 Nazionalità Coordinatore Turkey [TR]
 Totale costo 100˙000 €
 EC contributo 100˙000 €
 Programma FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
 Code Call FP7-PEOPLE-IRG-2008
 Funding Scheme MC-IRG
 Anno di inizio 2009
 Periodo (anno-mese-giorno) 2009-04-01   -   2013-03-31

 Partecipanti

# participant  country  role  EC contrib. [€] 
1    EGE UNIVERSITESI

 Organization address address: EGE UNIVERSITY KAMPUSU
city: IZMIR
postcode: 35040

contact info
Titolo: Prof.
Nome: Aysun
Cognome: Pabuccuoglu
Email: send email
Telefono: +90 532 3667701
Fax: +90 232 3885258

TR (IZMIR) coordinator 100˙000.00

Mappa


 Word cloud

Esplora la "nuvola delle parole (Word Cloud) per avere un'idea di massima del progetto.

pathways    first    erad    diseases    degradation    mechanism    er    cystic    substrates    aat    retrotranslocation    differences    deficiency    functional    fibrosis    interaction    substrate    misfolded    yeast    gp    regions    mammalian    protein   

 Obiettivo del progetto (Objective)

'The misfolded, unfolded or unassembled proteins in the Endoplasmic Reticulum (ER) are degraded by the “Protein Quality Control Mechanism” named as ER-associated degradation (ERAD). In addition to its safeguard role, ERAD can regulate physiological processes that occur in the ER, for example degradation of HMG–CoA reductase, the key enzyme of cholesterol synthesis. ERAD is a multistep process, which starts with substrate (unwanted protein) selection followed by ubiquitination, retrotranslocation, deglycosylation and proteasomal degradation. Aberrant ERAD has implications on several diseases, such as cystic fibrosis, a1-antitrypsin (AAT) deficiency, diabetes, neurodegenerative diseases and cancer. The details of ERAD mechanism are very well known through the studies in S.cerevisiae. Although the general scheme of the pathway is similar, ERAD is more complicated and highly regulated in mammals than in yeast. Studies in yeast suggested existence specialized ERAD pathways depending on the feature of the protein. These pathways are: ERAD-C ( for cytoplasmic misfolded domains), ERAD-L (for luminal misfolded regions), ERAD-M (for membrane misfolded regions). So far, this issue has not been studied in mammalian cells. Here, we intend to identify substrate specific differences present in retrotranslocation machineries in mammalian ERAD using four substrates with different structural features. Additionally, the effect of SVIP (the first identified endogenous ERAD inhibitor) on these substrates, the role of Npl4 in gp78-mediated ERAD and possible functional interaction of gp78 and hHrd1 enzymes will be examined. This research will provide the first information on the substrate specific differences of mammalian ERAD, and also the functional interaction between two important ER-resident E3s: gp78 and Hrd1. Our results on substrate specific ERAD mechanism would contribute to the studies on the therapies of diseases such as cystic fibrosis and AAT deficiency.'

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