Golgi glycosylation

Research output: Contribution to journalArticle

135 Citations (Scopus)

Abstract

Glycosylation is a very common modification of protein and lipid, and most glycosylation reactions occur in the Golgi. Although the transfer of initial sugar(s) to glycoproteins or glycolipids occurs in the ER or on the ER membrane, the subsequent addition of the many different sugars that make up a mature glycan is accomplished in the Golgi. Golgi membranes are studded with glycosyltransferases, glycosidases, and nucleotide sugar transporters arrayed in a generally ordered manner from the cis-Golgi to the trans-Golgi network (TGN), such that each activity is able to act on specific substrate(s) generated earlier in the pathway. The spectrum of glycosyltransferases and other activities that effect glycosylation may vary with cell type, and thus the final complement of glycans on glycoconjugates is variable. In addition, glycan synthesis is affected by Golgi pH, the integrity of Golgi peripheral membrane proteins, growth factor signaling, Golgi membrane dynamics, and cellular stress. Knowledge of Golgi glycosylation has fostered the development of assays to identify mechanisms of intracellular vesicular trafficking and facilitated glycosylation engineering of recombinant glycoproteins.

Original languageEnglish (US)
Pages (from-to)1-13
Number of pages13
JournalCold Spring Harbor perspectives in biology
Volume3
Issue number4
DOIs
StatePublished - Apr 2011

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Glycosylation
Sugars
Polysaccharides
Glycosyltransferases
Membranes
Glycoproteins
trans-Golgi Network
Glycoconjugates
Glycoside Hydrolases
Glycolipids
Assays
Intercellular Signaling Peptides and Proteins
Membrane Proteins
Nucleotides
Lipids
Substrates
Proteins

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Golgi glycosylation. / Stanley, Pamela.

In: Cold Spring Harbor perspectives in biology, Vol. 3, No. 4, 04.2011, p. 1-13.

Research output: Contribution to journalArticle

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