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Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase

Degradation of specific protein substrates by the anaphase-promoting complex/cyclosome (APC) is critical for mitotic exit. We have identified the protein Xenopus nuclear factor 7 (Xnf7) as a novel APC inhibitor able to regulate the timing of exit from mitosis. Immunodepletion of Xnf7 from Xenopus la...

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Autores principales: Casaletto, Jessica B., Nutt, Leta K., Wu, Qiju, Moore, Jonathan D., Etkin, Laurence D., Jackson, Peter K., Hunt, Tim, Kornbluth, Sally
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171901/
https://www.ncbi.nlm.nih.gov/pubmed/15824132
http://dx.doi.org/10.1083/jcb.200411056
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author Casaletto, Jessica B.
Nutt, Leta K.
Wu, Qiju
Moore, Jonathan D.
Etkin, Laurence D.
Jackson, Peter K.
Hunt, Tim
Kornbluth, Sally
author_facet Casaletto, Jessica B.
Nutt, Leta K.
Wu, Qiju
Moore, Jonathan D.
Etkin, Laurence D.
Jackson, Peter K.
Hunt, Tim
Kornbluth, Sally
author_sort Casaletto, Jessica B.
collection PubMed
description Degradation of specific protein substrates by the anaphase-promoting complex/cyclosome (APC) is critical for mitotic exit. We have identified the protein Xenopus nuclear factor 7 (Xnf7) as a novel APC inhibitor able to regulate the timing of exit from mitosis. Immunodepletion of Xnf7 from Xenopus laevis egg extracts accelerated the degradation of APC substrates cyclin B1, cyclin B2, and securin upon release from cytostatic factor arrest, whereas excess Xnf7 inhibited APC activity. Interestingly, Xnf7 exhibited intrinsic ubiquitin ligase activity, and this activity was required for APC inhibition. Unlike other reported APC inhibitors, Xnf7 did not associate with Cdc20, but rather bound directly to core subunits of the APC. Furthermore, Xnf7 was required for spindle assembly checkpoint function in egg extracts. These data suggest that Xnf7 is an APC inhibitor able to link spindle status to the APC through direct association with APC core components.
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spelling pubmed-21719012008-03-05 Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase Casaletto, Jessica B. Nutt, Leta K. Wu, Qiju Moore, Jonathan D. Etkin, Laurence D. Jackson, Peter K. Hunt, Tim Kornbluth, Sally J Cell Biol Research Articles Degradation of specific protein substrates by the anaphase-promoting complex/cyclosome (APC) is critical for mitotic exit. We have identified the protein Xenopus nuclear factor 7 (Xnf7) as a novel APC inhibitor able to regulate the timing of exit from mitosis. Immunodepletion of Xnf7 from Xenopus laevis egg extracts accelerated the degradation of APC substrates cyclin B1, cyclin B2, and securin upon release from cytostatic factor arrest, whereas excess Xnf7 inhibited APC activity. Interestingly, Xnf7 exhibited intrinsic ubiquitin ligase activity, and this activity was required for APC inhibition. Unlike other reported APC inhibitors, Xnf7 did not associate with Cdc20, but rather bound directly to core subunits of the APC. Furthermore, Xnf7 was required for spindle assembly checkpoint function in egg extracts. These data suggest that Xnf7 is an APC inhibitor able to link spindle status to the APC through direct association with APC core components. The Rockefeller University Press 2005-04-11 /pmc/articles/PMC2171901/ /pubmed/15824132 http://dx.doi.org/10.1083/jcb.200411056 Text en Copyright © 2005, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Research Articles
Casaletto, Jessica B.
Nutt, Leta K.
Wu, Qiju
Moore, Jonathan D.
Etkin, Laurence D.
Jackson, Peter K.
Hunt, Tim
Kornbluth, Sally
Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase
title Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase
title_full Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase
title_fullStr Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase
title_full_unstemmed Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase
title_short Inhibition of the anaphase-promoting complex by the Xnf7 ubiquitin ligase
title_sort inhibition of the anaphase-promoting complex by the xnf7 ubiquitin ligase
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2171901/
https://www.ncbi.nlm.nih.gov/pubmed/15824132
http://dx.doi.org/10.1083/jcb.200411056
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