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Cited by 203

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity

Open access
Abida, Wassim M., Nikolaev, Anatoly, Zhao, Wenhui, Zhang, Wenzhu, Gu, Wei·2007·Journal of Biological Chemistry

Abstract

The p53 tumor suppressor is regulated by post-translational modification, including ubiquitination, phosphorylation and acetylation. It has previously been shown that the ubiquitin ligase Mdm2 also promotes the conjugation of Nedd8, a ubiquitin-like protein, to p53, inhibiting its transcriptional activity. We report the identification of FBXO11, a member of the F-box protein family and a component of the Skp1.Cullin1.F-box (SCF) complex, as a new p53-interacting protein. We show that FBXO11 promotes the neddylation of p53 both in vitro and in vivo. In addition to the C-terminal lysine residues, FBXO11 can also promote Nedd8 conjugation to Lys-320 and Lys-321, and neddylation of p53 leads to suppression of p53 function. This is consistent with recent studies showing that a lysine to arginine mutation at Lys-320 significantly enhances p53 function, although Lys-320 was originally identified as an acetylation site involving PCAF-mediated activation of p53. Our study provides an example of an F-box protein acting as an adaptor protein that can mediate the neddylation of a non-cullin substrate.

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Metadata

Authors
Abida, W. M., Nikolaev, A., Zhao, W., Zhang, W., & Gu, W.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2007-01
Volume
282
Issue
3
Pages
1797-1804
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1998577031
Cited by
203
References
9
FWCI
4.19
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity. https://app.cochat.ai/papers/10.1074/jbc.m609001200
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Abida, W. M., Nikolaev, A., Zhao, W., Zhang, W., & Gu, W. (2007). FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m609001200

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