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Selective Autophagy Receptors Interact with EDEM1 During itsDegradation
Insook Jang,Sujin Park,Bruno Guhl,Jin Won Cho,Jürgen Roth 한국당과학회 2012 한국당과학회 학술대회 Vol.2012 No.1
EDEM1 is an endoplasmic reticulum-associated protein degradation (ERAD) component. ERAD is a cellular pathway that targets misfolded and misassembled glycoproteins for degradation. EDEM1 is involved in the recognition of misfolded luminal glycoproteins and in routing them for dislocation to the cytosol, followed by their degradation. EDEM1 interacts with substrate glycoproteins after their exit from the calnexin/calreticulin cycle and after processing by ER-mannosidase I. Although EDEM1 was proposed to be lectin–like and to react with Man8GlcNAc2 oligosaccharides, itsmechanism of action and its fate are still largely unknown. In a previous report, we found that EDEM1 becomes rapidly degraded and that this occurs by basal autophagy. Here, we show that EDEM1 forms complexes with the selective autophagy receptor p62, NBR1 and Alfy. This was demonstrated in HepG2 cells by double immunogold electron microscopy. Furthermore, we show the interaction between p62 and EDEM1 by immunoprecipitation- Western blot experiments. By serial section analysis, the origin of the phagophore for selective autophagy of EDEM1 could be identified as modified parts of rough ER cisternae. Hence, we provide new insight into the details of EDEM1 degradation process.
Protein N-Glycosylation, Protein Folding, and Protein Quality Control
Jürgen Roth,Christian Zuber,박수진,Insook Jang,Yangsin Lee,Katarina Gaplovska Kysela,Valérie Le Fourn,Roger Santimaria,Bruno Guhl,조진원 한국분자세포생물학회 2010 Molecules and cells Vol.30 No.6
Quality control of protein folding represents a funda-mental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.
Protein N-Glycosylation, Protein Folding, and Protein Quality Control
Roth, Jurgen,Zuber, Christian,Park, Su-Jin,Jang, In-Sook,Lee, Yang-Sin,Kysela, Katarina Gaplovska,Le Fourn, Valerie,Santimaria, Roger,Guhl, Bruno,Cho, Jin-Won Korean Society for Molecular and Cellular Biology 2010 Molecules and cells Vol.30 No.6
Quality control of protein folding represents a fundamental cellular activity. Early steps of protein N-glycosylation involving the removal of three glucose and some specific mannose residues in the endoplasmic reticulum have been recognized as being of importance for protein quality control. Specific oligosaccharide structures resulting from the oligosaccharide processing may represent a glycocode promoting productive protein folding, whereas others may represent glyco-codes for routing not correctly folded proteins for dislocation from the endoplasmic reticulum to the cytosol and subsequent degradation. Although quality control of protein folding is essential for the proper functioning of cells, it is also the basis for protein folding disorders since the recognition and elimination of non-native conformers can result either in loss-of-function or pathological-gain-of-function. The machinery for protein folding control represents a prime example of an intricate interactome present in a single organelle, the endoplasmic reticulum. Here, current views of mechanisms for the recognition and retention leading to productive protein folding or the eventual elimination of misfolded glycoproteins in yeast and mammalian cells are reviewed.