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).
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Antibodies / immunology
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Cell Cycle
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Cell Line
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Humans
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Jurkat Cells
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Oncogene Proteins / chemistry
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Oncogene Proteins / immunology
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Oncogene Proteins / metabolism*
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Retinoblastoma Protein / metabolism*
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Tumor Cells, Cultured
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Ubiquitin Thiolesterase
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Ubiquitin-Specific Proteases
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Ubiquitins / metabolism
Substances
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Antibodies
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Oncogene Proteins
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Retinoblastoma Protein
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USP4 protein, human
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Ubiquitins
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Ubiquitin Thiolesterase
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Ubiquitin-Specific Proteases