Editors' ChoiceReceptors

Helping Notch on Its Way

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Science's STKE  15 Mar 2005:
Vol. 2005, Issue 275, pp. tw98
DOI: 10.1126/stke.2752005tw98

Notch proteins act as receptors for a conserved signaling pathway affecting numerous cell fate decisions, and fucosylation of the glycans on Notch is thought to be important for its function. Okajima et al. (see the Perspective by Lowe) find that the fucosyl transferase, OFUT1, in addition to promoting fucosylation of a variety of substrates, including Notch, has a separable Notch-specific chaperone activity. It appears that OFUT1 binds to newly synthesized Notch receptors in the endoplasmic reticulum, where it promotes folding and thereby secretion of the Notch receptor. It is this chaperone function, not the ability to fucosylate the receptor, that is important in maintaining Notch function. It is possible that other glycosyl transferases may play similar roles in the quality control of other membrane and secretory proteins.

T. Okajima, A. Xu, L. Lei, K. D. Irvine, Chaperone activity of protein O-fucosyltransferase 1 promotes Notch receptor folding. Science 307, 1599-1603 (2005). [Abstract] [Full Text]

J. B. Lowe, Does Notch take the sweet road to success? Science 307, 1570-1572 (2005). [Summary] [Full Text]