Characterization of a protein export machinery of the endoplasmic reticulum
FP4 — Training and Mobility of Researchers
- Duration
- 1998-04-01 → 2000-03-31
- EU contribution
- —
- Participants
- 2
- Scheme
- RGI
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Project objective
Research objectives and content Selective proteolysis of aberrant or highly unstable proteins within the cytoplasm of eukaryotic cells depends on the ubiquitin/proteasome pathway. The same pathway has recently been shown to be also involved in the degradation of various proteins residing in the endoplasmic reticulum (ER). Integral proteins of the ER membrane may be be directly accessed by the ubiquitin/proteasome degradation machinery via their cytoplasmic domains. However, the breakdown of soluble proteins within the ER lumen and of the luminal parts of integral membran proteins must de. end on a so far unknown re-export apparatus, which specifically translocates these proteins into the cytoplasm prior to proteolytic degradation. The aim of this proposal is the characterization of factors required for the selective degradation of ER proteins and the isolation of components of a protein re-export machinery from the ER into the cytoplasm. The work will be carried out in the yeast Saccharomyces cerevisiae, which is suitable for genetic and biochemical analysis. Results obtained in the course of this work should provide general insights in the control and catalysis of the breakdown of proteins localized within cellular organelles. Training content (objective, benefit and expected impact) A research stay at the M.D.C. will help me to complement my present training in yeast genetics and microbiology with biochemical techniques and combine my experience obtained during the work on yeast mitochondrial biogenesis with the research on ER protein turnover. I will aquire new biochemical knowledge which will enable me to establish novel projects on eukaryotic organellar biogenesis in the future. Links with industry / industrial relevance (22)
Original text from CORDIS.
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Data: CORDIS, © European Union