MCDB428lect09 - MCDB 428 Lecture 9: Friday January 25, 2008...

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Lecture 9: Friday January 25, 2008 Today’s Outline N-linked Glycosylation Synthesis of the core precursor Inhibition by tunicamycin Trimming in the ER Surface Glycoproteins in Cell-Cell interaction Formation/Breakage of Disulfide Bonds Catalysis of disulfide bond formation PDI and Ero1 Protein Folding and Oligomerization Hemagglutinin (HA) function Role of disulfides in HA folding N-glycosyl trimming during HA folding Calnexin and glucosidase cycle during folding The unfolded protein response Defects in folding in disease MCDB 428
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Co-translational Translocation into ER What happens in ER after translocation is finished?
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ER Modifications N-linked Glycosylation Formation/Breakage of disulfide bonds Protein folding and oligomerization
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Asparagine Residues Can Be Glycosylated Asn residues are substrates for N- linked glycosylation in the ER This usually occurs on specific “glycosylation signal sequences,” Asn-X-Ser/Thr
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N-Glycosylation Occurs with a Pre-formed Core Polysaccharide Synthesis of the core polysaccharide occurs as a membrane anchored intermediate UDP-GlcNAc is added to dolichol phosphate and then six additional sugars are added to the precursor on the cytosolic side of the ER This partially formed precursor is then “flipped” to face the lumenal side of the ER and then the other seven sugars are added to the core on the lumenal side An antibiotic, tunicamycin , a general inhibitor of N-glycosylation, blocks the addition of the initial GlcNAc to dolichol phosphate
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This note was uploaded on 09/03/2009 for the course MCDB 428 taught by Professor Wang during the Winter '08 term at University of Michigan.

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MCDB428lect09 - MCDB 428 Lecture 9: Friday January 25, 2008...

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