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ER Tail-Anchored Proteins Integration
In this lecture ´´ Protein Translocation via ER ´´ is explained. Section one is about ´´ ER Tail-Anchored Proteins Integration´´. In the start of this lecture, translocated polypeptide chains are discussed. After that, protein disulphide isomerase (PDI) is introduced. Lastly, chaperone protein BiP is made a part of discussion.
Section two is about “Glycosylation”. Initially, N- linked or asparagine linked glycosylation is explained. The educator then talks about oligosaccharide trimming or processing along with O-linked oligosaccharide glycosylation. Calnexin and calreticulin are also elucidated in this section. In the end, the educator explains how oligosaccharides are used as tags.
Fate of Improperly Folded Proteins
Section three is about ‘Fate of Improperly Folded Proteins“. This section is started with the explanation of retrotranslocation. The misfolded proteins are demonstrated and recognition of misfolded or unfolded proteins are thoroughly explained. Finishing this section, the educator talks about multiple translocator complexes.
Misfolded Proteins in ER
Section four is about ‘’ Misfolded Proteins in ER’’. Starting with the discussion on how misfolded proteins in ER signal to nucleus. Also, the activation of second transmembrane kinase is discussed in the end.
Lipid Bilayer Assembly
Section five is about “Lipid Bilayer Assembly’’. It discusses glycosylphosphatidylinositol anchor in the beginning. The educator then talks about how ER assembles lipid bilayers. Scrambalase and flippases are then elucidated. After that, cholesterol and ceramide is explained. In the end of this lecture, transport vesicles network and phospholipid exchange proteins are demonstrated.