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- Title
O-GlcNAcase is Cleaved Between Its Glycosidase & Histone Acetyltransferase Domains by Caspase-3 During Apoptosis.
- Authors
Butkinaree, Chutikarn; Cheung, Win D.; Kyoungsook Park; Hart, Gerald W.
- Abstract
O-GlcNAc is a dynamic post-translational modification on many nucleocytoplasmic proteins, ranging from transcription factors, signaling proteins, to cytoskeletal proteins. O-GlcNAc is a nutrient sensor involved in the regulation of cellular activity, including transcription, response to stress, and protein-protein interactions. Recent studies have shown that O-GlcNAc cycling is affected by apoptosis induction. O-GlcNAcase, the O-GlcNAc removal enzyme, has been shown to be a substrate ofcaspase-3 in vitro. Here we identify the cleavage site of O-GlcNAcase by caspase-3 using Edman sequencing. A point mutation at the cleavage site abrogates cleavage by caspase-3 in vitro. We also show that O-GlcNAcase is a substrate of caspase-3 during Fas-mediated apoptosis in vivo in various cell lines separating the two functional domains of this bi-functional enzyme. Interestingly, caspase-3 cleavage does not affect the activity of the enzyme nor its localization. We are currently investigating how O-GlcNAcase cleavage by caspase-3 is involved in the apoptotic events using the mutant lacking a caspase-3 cleavage site during apoptotic induction. These data will give a better understanding of how O-GlcNAc and O-GlcNAcase are involved in the regulation of apoptosis.
- Subjects
PROTEINS; ACETYLTRANSFERASES; GLYCOSIDASES; HISTONES; PROTEOLYTIC enzymes; APOPTOSIS
- Publication
FASEB Journal, 2007, Vol 21, Issue 5, pA257
- ISSN
0892-6638
- Publication type
Article