Lecture 11 - protein modification and degradation

Lecture 11 - protein modification and degradation -...

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Unformatted text preview: Glycosylation The mechanisms for glycosylation are complex but many common features exist. 1.Needs activated sugars. UDP-glucose, UDP-galactosamine, UDP-N acetylglucosamine, GDP-mannose. etc. 2.Takes place in ER and Golgi apparatus. 3.The synthesis of O-glycosidically linked glycoproteins involves the sequential action of a series of glycosyl transferases. 4. The synthesis of N-glycosidically linked glycoproteins involves the transfer of oligosaccharide mediated by dolichol pyrophosphate, a membrane bound lipid. 5. The N-glycosylation of the specific asparagine residue (ASN-X-Ser or ASN- X-Thr) of the nascent polypeptide may occur in the luman of the ER. O- glycosylation of specific serine or threonine residue occurs after the polypeptide has transported into the Golgi apparatus. O-glycosylation of hydroxylysine residue by specific galactosyltransferase occurs in the ER. 6. Further processing the oligosaccharide, addition and removal of glycosyl residue also takes place in both the ER and Golgi apparatus ER Golgi The presence of mannose 6- phosphate residues is the structural signal that targets the protein to lysosomes. Further Posttranslational protein modifications:...
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This note was uploaded on 10/13/2011 for the course NS 3200 at Cornell University (Engineering School).

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Lecture 11 - protein modification and degradation -...

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