CBIO 3400 Lecture Notes - Lecture 3: Secretion, Glycan, Protein Folding
Document Summary
Today"s class: protein modifications in the er, n-glycosylation of proteins, protein folding. Big picture-understand how proteins that initially start in the cytoplasm get sent to the er. Protein modifications that can occur in er: proteolytic processing, protein glycosylation (enzymes add sugars in er)- see effects of timing of the protein leaving the er, protein folding, chaperons can facilitate proper folding of protein, disulfide bond formation. *carried out by er-resident proteins (meant to be er proteins) Kind of protects them: other functions, allows for proteins to be involved in cell to cell adhesion. Important of immune responses: pathway is very important for congenital disorders of n-linked glycosylation results in a variety of very serious symptoms, symptoms are very severe and often lead to death. Protein glycosylation n-linked glycans: begins in er with additional of large precursor, glc= glucose, man= mannose, glcnac= n-acetylglucosasmine, glc1 manq (glcnac)2 (large precursor) stay in er, to asn-x-ser/thr, continues in er and golgi with oligo processing.