Protein substrates engage the lumen of O-GlcNAc transferase's tetratricopeptide repeat domain in different ways
CM Joiner, FA Hammel, J Janetzko, S Walker - Biochemistry, 2021 - ACS Publications
Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational
modification in mammals. O-GlcNAc transferase (OGT), the sole enzyme responsible for this
modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates. How
OGT selects its substrates is a fundamental question that must be answered to understand
OGT's unusual biology. OGT contains a long tetratricopeptide repeat (TPR) domain that has
been implicated in substrate selection, but there is almost no information about how …
modification in mammals. O-GlcNAc transferase (OGT), the sole enzyme responsible for this
modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates. How
OGT selects its substrates is a fundamental question that must be answered to understand
OGT's unusual biology. OGT contains a long tetratricopeptide repeat (TPR) domain that has
been implicated in substrate selection, but there is almost no information about how …
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