Addition of a bifurcating GlcNAc to the N-glycan by MGAT3

Stable Identifier
Reaction [transition]
Homo sapiens
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The addition of a bisecting GlcNAc to a complex N-glycan by MGAT3 is one of the most important regulatory steps in N-glycosylation, directing the pathway toward the synthesis of complex and hybrid N-glycans. This addition changes the structure of the N-glycan and inhibits further modification by MGAT2, MGAT4, MGAT5A/B and FUT8. Defects in MGAT3 have been shown to be associated with predisposition to cancer and several developmental defects (Song et al 2010; Stanley 2002).

Literature References
PubMed ID Title Journal Year
12417419 Biological consequences of overexpressing or eliminating N-acetylglucosaminyltransferase-TIII in the mouse

Stanley, P

Biochim Biophys Acta 2002
20395209 The bisecting GlcNAc on N-glycans inhibits growth factor signaling and retards mammary tumor progression

Aglipay, JA, Bernstein, JD, Stanley, P, Song, Y, Goswami, S

Cancer Res 2010
Catalyst Activity

beta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity of MGAT3 [Golgi membrane]

Orthologous Events
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