The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein

Lauren M. Desalle; Esther Latres; Douglas Lin; Edgard Graner; Alessia Montagnoli; Rohan T. Baker; Michele Pagano; Massimo Loda

doi:10.1038/sj.onc.1204824

The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein

Lauren M. Desalle, Esther Latres, Douglas Lin, Edgard Graner, Alessia Montagnoli, Rohan T. Baker, Michele Pagano, Massimo Loda^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

31 Citations (Scopus)

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).

Original language	English
Pages (from-to)	5538-5542
Number of pages	5
Journal	Oncogene
Volume	20
Issue number	39
DOIs	https://doi.org/10.1038/sj.onc.1204824
Publication status	Published - 6 Sept 2001

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title = "The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein",

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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AU - Desalle, Lauren M.

AU - Latres, Esther

AU - Lin, Douglas

AU - Graner, Edgard

AU - Montagnoli, Alessia

AU - Baker, Rohan T.

AU - Pagano, Michele

AU - Loda, Massimo

PY - 2001/9/6

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AB - 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).

KW - Isopeptidase

KW - Retinoblastoma

KW - Ubiquitin

KW - Unp

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VL - 20

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JO - Oncogene

JF - Oncogene

IS - 39

ER -

The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein

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