| Non-degradative Ubiquitination of AIF by XIAP at a Residue Critical for AIF-mediated Chromatin Degradation. | |
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MedLine Citation:
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PMID: 22103349 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Apoptosis inducing factor (AIF) is a mediator of caspase-independent cell death that is also necessary for mitochondrial energy production. How these seemingly opposite cellular functions of AIF are controlled is poorly understood. X-linked inhibitor of apoptosis (XIAP) is an endogenous inhibitor of caspases that also regulates several caspase-independent signaling pathways. The RING domain of XIAP possesses E3 ubiquitin-ligase activity, though the importance of this function to signal regulation remains incompletely defined. XIAP binds and ubiquitinates AIF, and in this study we determined the functional consequences of XIAP-mediated AIF ubiquitination. Unlike canonical ubiquitination, XIAP-dependent AIF ubiquitination did not lead to proteasomal degradation of AIF. Experiments using ubiquitin mutants demonstrated that the XIAP-dependent ubiquitin linkage was not formed through the commonly used lysine 48, suggesting a non-canonical ubiquitin linkage is employed. Further studies demonstrated that only lysine 255 of AIF was a target of XIAP-dependent ubiquitination. Using recombinant AIF we determined that mutating lysine 255 of AIF interferes with the ability of AIF to not only bind DNA but also degrade chromatin in vitro. These data indicate that XIAP regulates the death-inducing activity of AIF through non-degradative ubiquitination, further defining the role of XIAP in controlling AIF and caspase-independent cell death pathways. |
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Authors:
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Eric M Lewis; Amanda S Wilkinson; Nichole Davis; David A Horita; John Curlee Wilkinson |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-11-21 |
Journal Detail:
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Title: Biochemistry Volume: - ISSN: 1520-4995 ISO Abbreviation: - Publication Date: 2011 Nov |
Date Detail:
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Created Date: 2011-11-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0370623 Medline TA: Biochemistry Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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