First Author | Hauser HP | Year | 1998 |
Journal | J Cell Biol | Volume | 141 |
Issue | 6 | Pages | 1415-22 |
PubMed ID | 9628897 | Mgi Jnum | J:48143 |
Mgi Id | MGI:1266878 | Doi | 10.1083/jcb.141.6.1415 |
Citation | Hauser HP, et al. (1998) A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J Cell Biol 141(6):1415-22 |
abstractText | Ubiquitin-conjugating enzymes (UBC) catalyze the covalent attachment of ubiquitin to target proteins and are distinguished by the presence of a UBC domain required for catalysis. Previously identified members of this enzyme family are small proteins and function primarily in selective proteolysis pathways. Here we describe BRUCE (BIR repeat containing ubiquitin-conjugating enzyme), a giant (528-kD) ubiquitin-conjugating enzyme from mice. BRUCE is membrane associated and localizes to the Golgi compartment and the vesicular system. Remarkably, in addition to being an active ubiquitin-conjugating enzyme, BRUCE bears a baculovirus inhibitor of apoptosis repeat (BIR) motif, which to this date has been exclusively found in apoptosis inhibitors of the IAP-related protein family. The BIR motifs of IAP proteins are indispensable for their anti-cell death activity and are thought to function through protein-protein interaction. This suggests that BRUCE may combine properties of IAP-like proteins and ubiquitin- conjugating enzymes and indicates that the family of IAP-like proteins is structurally and functionally more diverse than previously expected. |