Regulation of the Copper Chaperone CCS by XIAP-Mediated Ubiquitination
Autor: | Kojo S.J. Elenitoba-Johnson, Xuwen Liu, Graham F. Brady, Jonathan D. Gitlin, Colin S. Duckett, Stefanie Galbán, Venkatesha Basrur, Thomas E. Wilson |
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Rok vydání: | 2010 |
Předmět: |
Saccharomyces cerevisiae Proteins
X-Linked Inhibitor of Apoptosis Protein Biology Inhibitor of apoptosis Cell Line Superoxide dismutase Mice Enzyme activator Superoxide Dismutase-1 Ubiquitin Animals Humans Tissue Distribution Molecular Biology Mice Knockout Superoxide Dismutase fungi Ubiquitination Articles Cell Biology XIAP Ubiquitin ligase Enzyme Activation Mice Inbred C57BL Copper chaperone for superoxide dismutase Biochemistry Chaperone (protein) biology.protein biology.gene Copper Molecular Chaperones |
Zdroj: | Molecular and Cellular Biology. 30:1923-1936 |
ISSN: | 1098-5549 |
DOI: | 10.1128/mcb.00900-09 |
Popis: | In order to balance the cellular requirements for copper with its toxic properties, an elegant set of mechanisms has evolved to regulate and buffer intracellular copper. The X-linked inhibitor of apoptosis (XIAP) protein was recently identified as a copper-binding protein and regulator of copper homeostasis, although the mechanism by which XIAP binds copper in the cytosol is unclear. Here we describe the identification of the copper chaperone for superoxide dismutase (CCS) as a mediator of copper delivery to XIAP in cells. We also find that CCS is a target of the E3 ubiquitin ligase activity of XIAP, although interestingly, ubiquitination of CCS by XIAP was found to lead to enhancement of its chaperone activity toward its physiologic target, superoxide dismutase 1, rather than proteasomal degradation. Collectively, our results reveal novel links among apoptosis, copper metabolism, and redox regulation through the XIAP-CCS complex. |
Databáze: | OpenAIRE |
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