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Cited by 194

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53

Open access
Rajendra, Rajeev, Malegaonkar, Diptee, Pungaliya, Pooja, Marshall, Henderson, Rasheed, Zeshaan, Brownell, James, Liu, Leroy F., Lutzker, Stuart, Saleem, Ahamed, Rubin, Eric H.·2004·Journal of Biological Chemistry

Abstract

The human topoisomerase I- and p53-binding protein topors contains a highly conserved, N-terminal C3HC4-type RING domain that is homologous to the RING domains of known E3 ubiquitin ligases. We demonstrate that topors functions in vitro as a RING-dependent E3 ubiquitin ligase with the E2 enzymes UbcH5a, UbcH5c, and UbcH6 but not with UbcH7, CDC34, or UbcH2b. Additional studies indicate that a conserved tryptophan within the topors RING domain is required for ubiquitination activity. Furthermore, both in vitro and cellular studies implicate p53 as a ubiquitination substrate for topors. Similar to MDM2, overexpression of topors results in a proteasome-dependent decrease in p53 protein expression in a human osteosarcoma cell line. These results are similar to the recent finding that a Drosophila topors orthologue ubiquitinates the Hairy transcriptional repressor and suggest that topors functions as a ubiquitin ligase for multiple transcription factors.

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Metadata

Authors
Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z., Brownell, J., Liu, L. F., Lutzker, S., Saleem, A., & Rubin, E. H.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2004-08
Volume
279
Issue
35
Pages
36440-36444
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2069078243
Cited by
194
References
5
FWCI
4.26
Type
journal article
Language
en
Open access
hybrid

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Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z., Brownell, J., Liu, L. F., Lutzker, S., Saleem, A., & Rubin, E. H. (2004). Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c400300200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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