FIGURE 18.3. O-GlcNAc cycling is regulated by the concerted action of O-GlcNAc transferase (OGT) and O-GlcNAcase.

FIGURE 18.3

O-GlcNAc cycling is regulated by the concerted action of O-GlcNAc transferase (OGT) and O-GlcNAcase. OGT has two distinct domains: the transferase domain, which contains the catalytic site and is related to glycogen phosphorylase, and the tetratricopeptide repeat (TPR) domain, which contains protein:protein interaction sites. O-GlcNAcase also has two functional domains, which are separated by a caspase-3 cleavage site. O-GlcNAcase has an active histone acetyltransferase (HAT) domain at its carboxyl terminus and an N-acetylglucosaminidase domain at its amino terminus. (Redrawn, with permission, from Slawson C., Housley M.P., and Hart G.W. 2006. J. Cell. Biochem. 97: 71–83.)

From: Chapter 18, The O-GlcNAc Modification

Cover of Essentials of Glycobiology
Essentials of Glycobiology. 2nd edition.
Varki A, Cummings RD, Esko JD, et al., editors.
Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 2009.
Copyright © 2009, The Consortium of Glycobiology Editors, La Jolla, California.

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