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Glycosylation-directed quality control of protein folding

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 16, Issue 12, Pages 742-752

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm4073

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Funding

  1. Temasek Trust

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Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated in the endoplasmic reticulurn. These adducts have many biological functions, including, notably, their contribution to the maturation of glycoproteins. N-linked glycans are of oligomeric structure, forming configurations that provide blueprints to precisely instruct the folding of protein substrates and the quality control systems that scrutinize it. O-linked mannoses are simpler in structure and were recently found to have distinct functions in protein quality control that do not require the complex structure of N-linked glycans. Together, recent studies reveal the breadth and sophistication of the roles of these glycan-directed modifications in protein biogenesis.

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