Botch Is a γ-Glutamyl Cyclotransferase that Deglycinates and Antagonizes Notch

17Citations
Citations of this article
36Readers
Mendeley users who have this article in their library.

Abstract

Botch promotes embryonic neurogenesis by inhibiting the initial S1 furin-like cleavage step of Notch maturation. The biochemical process by which Botch inhibits Notch maturation is not known. Here, we show that Botch has γ-glutamyl cyclotransferase (GGCT) activity that deglycinates Notch, which prevents the S1 furin-like cleavage. Moreover, Notch is monoglycinated on the γ-glutamyl carbon of glutamate 1,669. The deglycinase activity of Botch is required for inhibition of Notch signaling both in vitro and in vivo. When the γ-glutamyl-glycine at position 1,669 of Notch is degylcinated, it is replaced by 5-oxy-proline. These results reveal that Botch regulates Notch signaling through deglycination and identify a posttranslational modification of Notch that plays an important role in neurogenesis. © 2014 The Authors.

Cite

CITATION STYLE

APA

Chi, Z., Byrne, S. T., Dolinko, A., Harraz, M. M., Kim, M. S., Umanah, G., … Dawson, V. L. (2014). Botch Is a γ-Glutamyl Cyclotransferase that Deglycinates and Antagonizes Notch. Cell Reports, 7(3), 681–688. https://doi.org/10.1016/j.celrep.2014.03.048

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free