Fringe-modified Pre-NOTCH is cleaved by FURIN

Stable Identifier
Reaction [transition]
Homo sapiens
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Cleavage of fringe-modified NOTCH by FURIN has not been examined directly, but since mature, plasma membrane-anchored NOTCH receptors are typically cleaved by FURIN (Blaumueller et al. 1997) and fringe-modified NOTCH functions at the cell surface (Moloney et al. 2000), it is expected that fringe-modified NOTCH is processed by FURIN cleavage. The exact order of fringe-mediated glycosylation and FURIN cleavage has not been experimentally established, but since FURIN localizes to the trans-Golgi network -TGN (Teuchert et al. 1999), while fringe has not been associated with TGN, it is likely that modification of NOTCH by fringe enzymes precedes FURIN-mediated cleavage.

Literature References
PubMed ID Title Journal Year
10075724 Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins

Hoflack, B, Klenk, HD, Garten, W, Schäfer, W, Berghöfer, S, Teuchert, M

J Biol Chem 1999
10935626 Fringe is a glycosyltransferase that modifies Notch

Shao, L, Wang, Y, Johnston, SH, Irvine, KD, Stanley, P, Haltiwanger, RS, Moloney, DJ, Wilson, R, Chen, J, Vogt, TF, Panin, VM

Nature 2000
9244302 Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane

Artavanis-Tsakonas, S, Zagouras, P, Qi, H, Blaumueller, CM

Cell 1997
Catalyst Activity

serine-type endopeptidase activity of FURIN [Golgi membrane]

Orthologous Events
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