Abstract：
:Fucose is a common terminal modification on protein and lipid glycans. Fucose can also be directly linked to protein via an O-linkage to Serine or Threonine residues located within consensus sequences contained in Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). In this context, fucose is added exclusively to properly folded EGF repeats and TSRs by Protein O-fucosyltransferases 1 and 2, respectively. In both cases, the O-linked fucose can also be elongated with other sugars. Here, we describe the biological importance of these O-fucose glycans and molecular mechanisms by which they affect the function of the proteins they modify. O-Fucosylation of EGF repeats modulates the Notch signaling pathway, while O-fucosylation of TSRs is predicted to influence secretion of targets including several extracellular proteases. Recent data show O-fucose glycans mediate their effects by participating in both intermolecular and intramolecular interactions.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Holdener BC,Haltiwanger RSdoi
10.1016/j.sbi.2018.12.005subject
Has Abstractpub_date
2019-06-01 00:00:00pages
78-86eissn
0959-440Xissn
1879-033Xpii
S0959-440X(18)30153-2journal_volume
56pub_type
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journal_title：Current opinion in structural biology
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