Abstract
In all eukaryotic cells secretory proteins and cell surface receptors are synthesized on ribosomes attached to the rough endoplasmic reticulum (ER) (15). The growing Polypeptide chain is extruded from the ribosome and transported in an unfolded state through a protein- lined channel in the ER membrane into the ER lumen; it is never exposed to the cytosol. Secretory proteins are completely transported into the ER lumen; membrane proteins become anchored in the ER membrane via one or more ∼23 amino acid hydrophobic segments that form membrane- spanning a- helixes. Once synthesis is complete, newly introduced Polypeptides in the membrane and lumen of the ER must be folded, matured, sorted, and transported. Secretory or membrane proteins undergo many modifications during their transit to the cell surface:
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(i)
cleavage of signal sequences
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(ii)
formation and rearrangement of disulfide bonds
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(iii)
other protein folding steps, including formation of muluchain proteins
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(iv)
addition and modification of N- and O- linked Oligosaccharides
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(v)
other specific proteolytic cleavages.
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Lodish, H.F. (1997). Biogenesis of Secretory Proteins and Cell Surface Receptors in Mammalian Cells: Posttranslational Modifications and Protein Folding within the Rough Endoplasmic Reticulum. In: Carrondo, M.J.T., Griffiths, B., Moreira, J.L.P. (eds) Animal Cell Technology. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5404-8_3
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DOI: https://doi.org/10.1007/978-94-011-5404-8_3
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