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The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein

Oncogene volume 20, pages 5538–5542 (2001)Cite this article

Abstract

The ubiquitin pathway is involved in the proteolytic turnover of many short-lived cellular regulatory proteins. Since selective degradation of substrates of this system requires the covalent attachment of a polyubiquitin chain to the substrates, degradation could be counteracted by de-ubiquitinating enzymes (or isopeptidases) which selectively remove the polyubiquitin chain. Unp is a human isopeptidase with still poorly understood biological functions. Here, we show that cellular Unp specifically interacts with the retinoblastoma gene product (pRb).

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Acknowledgements

We thank G Draetta and D Gray for reagents. This work was supported by grants from the Human Frontier Science Program Organization (RG0229), by a Irma T Hirschl Scholarship and NIH grants (R01-CA76584, R01-GM57587, P30-CA16087 and R21-CA66229) to M Pagano, and the NIH grant 5RO1-CA81755 to M Loda.

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Authors and Affiliations

  1. Department of Pathology and Kaplan Comprehensive Cancer Center, MSB 548, New York University Medical Center, 550 First Avenue, New York, NY 10016, USA

    Lauren M DeSalle, Esther Latres, Alessia Montagnoli & Michele Pagano

  2. Department of Adult Oncology, Dana Farber Cancer Institute, Boston, Massachusetts, USA

    Douglas Lin, Edgard Graner & Massimo Loda

  3. Department of Pathology, Brigham & Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA

    Massimo Loda

  4. John Curtin School of Medical Research, Australian National University, Canberra, Australia

    Rohan T Baker

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  1. Lauren M DeSalle
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DeSalle, L., Latres, E., Lin, D. et al. The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein. Oncogene 20, 5538–5542 (2001). https://doi.org/10.1038/sj.onc.1204824

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