Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking

Misfolded, luminal endoplasmic reticulum (ER) proteins must be recognized before being degraded by a process called ERAD-L. Using site-specific photocrosslinking in Saccharomyces cerevisiae, we tested luminal interactions of a glycosylated ERAD-L substrate with potential recognition components. Majo...

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Veröffentlicht in:	FEBS letters 2011-05, Vol.585 (9), p.1281-1286
Hauptverfasser:	Stanley, Ann Marie, Carvalho, Pedro, Rapoport, Tom
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites carboxypeptidase Y Carrier Proteins - genetics Carrier Proteins - metabolism CPY Cross-Linking Reagents - metabolism crosslinking Der1p DHFR dihydrofolate reductase Endoplasmic reticulum Endoplasmic Reticulum - metabolism endoplasmic reticulum-associated degradation ER-associated degradation ERAD glycosylation hemagglutinin Hrd3p Immunoblotting Immunoprecipitation lectins Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Misfolded proteins Multiprotein Complexes - metabolism polypeptides Protein Binding - radiation effects Protein Folding Protein Transport Recombinant Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism sCPY short carboxypeptidase Y Substrate Specificity Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ultraviolet Rays Yos9p
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