BIO230H1 Lecture Notes - Lecture 11: Tethering, Gtpase, Hydrolysis

• School: UTSG
• Department: Biology
• Course: BIO230H1
• Professor: Darrell Desveaux Tony Harris

Document Summary

Thursday, october 12th, 2017 1pm-2pm (alberts et al. Lecture 11 outline: protein sorting, continue with protein sorting already talking about transmembrane transport with translocator complexes, for the mitochondria, chloroplasts, er. Transport into the er is co-translational, especially for all transmembrane proteins: want to look at how proteins are sorted from the er into the other compartments using, glycosylation, molecular mechanisms. First, we"ll look at what happens to proteins once they make it into the er: almost all of them are glycosylation (addition of sugars) Glycosylation: most soluble and transmembrane proteins in er are glycosylated, two types, o-linked glycosylation (ser. Thr: n-linked glycosylation (asn, n-linked oligosaccharide precursor, pre-formed in the er, linked to target protein in rer, most soluble and transmembrane proteins that enter the er are glycosylated. N-linked protein glycosylation in the rough er : almost as soon as a polypeptide chain enters the er lumen, it"s glycosylated on target asn residues.