Regulation of apoptosis and cytokinesis by the anti-apoptotic E2/E3 ubiquitin-ligase BRUCE.
Members of the inhibitor of apoptosis protein (IAP) family are key regulators of apoptosis as they bind and inhibit caspases and other pro-apoptotic factors. Recent findings suggest that these proteins play additional roles, e.g., in cell cycle regulation, angiogenesis, and carcinogenesis. Here, we review the function of BRUCE (BIR repeat-containing ubiquitin-conjugating enzyme), an unusual 528-kDa IAP with ubiquitin ligase activity, and describe its role in apoptosis and cytokinesis. Additionally, we discuss how these seemingly unrelated functions might be linked.
Pohl
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Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany. cpohl@biochem.mpg.de
Jentsch
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D000818:Animals; D017209:Apoptosis; D048749:Cytokinesis; D005786:Gene Expression Regulation; D006801:Humans; D051034:Inhibitor of Apoptosis Proteins / Q000235:genetics / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
D051034:Inhibitor of Apoptosis Proteins; D044763:Ubiquitin-Conjugating Enzymes; D044767:Ubiquitin-Protein Ligases