Structural highlights
Function
[UBE2Z_HUMAN] Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation.[PROSITE-ProRule:PRU00388][1] [2]
Publication Abstract from PubMed
FAT10 conjugation, a post-translational modification analogous to ubiquitination, specifically requires UBA6 and UBE2Z as its activating (E1) and conjugating (E2) enzymes. Interestingly, these enzymes can also function in ubiquitination. We have determined the crystal structure of UBE2Z and report how the different domains of this E2 enzyme are organized. We further combine our structural data with mutational analyses to understand how specificity is achieved in the FAT10 conjugation pathway. We show that specificity towards UBA6 and UBE2Z lies within the C-terminal CYCI tetra-peptide in FAT10. We also demonstrate that this motif slows down transfer rates for FAT10 from UBA6 onto UBE2Z.
Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery.,Schelpe J, Monte D, Dewitte F, Sixma TK, Rucktooa P J Biol Chem. 2015 Nov 10. pii: jbc.M115.671545. PMID:26555268[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park KM, Kang E, Jeon YJ, Kim N, Kim NS, Yoo HS, Yeom YI, Kim SJ. Identification of novel regulators of apoptosis using a high-throughput cell-based screen. Mol Cells. 2007 Apr 30;23(2):170-4. PMID:17464193
- ↑ Jin J, Li X, Gygi SP, Harper JW. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature. 2007 Jun 28;447(7148):1135-8. PMID:17597759 doi:http://dx.doi.org/nature05902
- ↑ Schelpe J, Monte D, Dewitte F, Sixma TK, Rucktooa P. Structure of UBE2Z provides functional insight into specificity in the FAT10 conjugation machinery. J Biol Chem. 2015 Nov 10. pii: jbc.M115.671545. PMID:26555268 doi:http://dx.doi.org/10.1074/jbc.M115.671545
