BIO 320 Lecture Notes - Lecture 6: Glycosylation, Protein Folding, Disulfide
Document Summary
Disulfide bond formation on some by (p isomerase) Most become n-linked glycosylated and undergo glucose trimming. Erad - er-associated degradation - exportation to cytosol of misfolded proteins (poly-ubiquitination proteasome) *only properly folded proteins leave the er for the golgi. Many (not all) cell types - er-derived transport vesicles fuse with each other to form the vesicular tubular cluster which becomes the cis -golgi (network) Moved along microtubules carries by motor protein (kinesin and others) Specific (mostly transmembrane) proteins are concentrated in distinct golgi sub-compartments, including many enzymes that modify proteins that are on their way from the cgn ( cis -golgi network) to the tgn ( trans -golgi network) (earlier later) The concentration and presence of these specific proteins define the different. Wrong model - vesicular transport model - budding by copi-coated vesicle from each sub-compartment in the golgi moves forward via anterograde transport and return same process with retrograde movement.
