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A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors

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Hauser,  H-P
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Bardroff,  M
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Pyrowolakis,  G
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Jentsch,  S
Jentsch Group, Friedrich Miescher Laboratory, Max Planck Society;

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Citation

Hauser, H.-P., Bardroff, M., Pyrowolakis, G., & Jentsch, S. (1998). A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. The Journal of Cell Biology, 141(6), 1415-1422. doi:10.1083/jcb.141.6.1415.


Cite as: https://hdl.handle.net/21.11116/0000-000A-DD1D-E
Abstract
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.