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  1. Article ; Online: Protein partners of deubiquitinating enzymes.

    Ventii, Karen H / Wilkinson, Keith D

    The Biochemical journal

    2008  Volume 414, Issue 2, Page(s) 161–175

    Abstract: Protein modification by ubiquitin and ubiquitin-like molecules is a critical regulatory process. Like most regulated protein modifications, ubiquitination is reversible. Deubiquitination, the reversal of ubiquitination, is quickly being recognized as an ... ...

    Abstract Protein modification by ubiquitin and ubiquitin-like molecules is a critical regulatory process. Like most regulated protein modifications, ubiquitination is reversible. Deubiquitination, the reversal of ubiquitination, is quickly being recognized as an important regulatory strategy. Nearly one hundred human DUBs (deubiquitinating enzymes) in five different gene families oppose the action of several hundred ubiquitin ligases, suggesting that both ubiquitination and its reversal are highly regulated and specific processes. It has long been recognized that ubiquitin ligases are modular enzyme systems that often depend on scaffolds and adaptors to deliver substrates to the catalytically active macromolecular complex. Although many DUBs bind ubiquitin with reasonable affinities (in the nM to microM range), a larger number have little affinity but exhibit robust catalytic capability. Thus it is apparent that these DUBs must acquire their substrates by binding the target protein in a conjugate or by associating with other macromolecular complexes. We would then expect that a study of protein partners of DUBs would reveal a variety of substrates, scaffolds, adaptors and ubiquitin receptors. In the present review we suggest that, like ligases, much of the regulation and specificity of deubiquitination arises from the association of DUBs with these protein partners.
    MeSH term(s) Endopeptidases/metabolism ; Humans ; Proteasome Endopeptidase Complex/metabolism ; Protein Binding ; Proteins ; Ubiquitin/metabolism ; Ubiquitin Thiolesterase/metabolism ; Ubiquitination
    Chemical Substances Proteins ; Ubiquitin ; Endopeptidases (EC 3.4.-) ; Ubiquitin Thiolesterase (EC 3.4.19.12) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2008-08-08
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BJ20080798
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes.

    Reyes-Turcu, Francisca E / Ventii, Karen H / Wilkinson, Keith D

    Annual review of biochemistry

    2009  Volume 78, Page(s) 363–397

    Abstract: Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene products, reverse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-like) chains on target proteins. The human genome ... ...

    Abstract Deubiquitinating enzymes (DUBs) are proteases that process ubiquitin or ubiquitin-like gene products, reverse the modification of proteins by a single ubiquitin(-like) protein, and remodel polyubiquitin(-like) chains on target proteins. The human genome encodes nearly 100 DUBs with specificity for ubiquitin in five gene families. Most DUB activity is cryptic, and conformational rearrangements often occur during the binding of ubiquitin and/or scaffold proteins. DUBs with specificity for ubiquitin contain insertions and extensions modulating DUB substrate specificity, protein-protein interactions, and cellular localization. Binding partners and multiprotein complexes with which DUBs associate modulate DUB activity and substrate specificity. Quantitative studies of activity and protein-protein interactions, together with genetic studies and the advent of RNAi, have led to new insights into the function of yeast and human DUBs. This review discusses ubiquitin-specific DUBs, some of the generalizations emerging from recent studies of the regulation of DUB activity, and their roles in various cellular processes.
    MeSH term(s) Animals ; Endopeptidases/chemistry ; Endopeptidases/genetics ; Endopeptidases/metabolism ; Humans ; Protein Structure, Tertiary ; Ubiquitin/genetics ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Ubiquitin ; Endopeptidases (EC 3.4.-)
    Keywords covid19
    Language English
    Publishing date 2009-06-02
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev.biochem.78.082307.091526
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: The ubiquitin signal: assembly, recognition and termination. Symposium on ubiquitin and signaling.

    Wilkinson, Keith D / Ventii, Karen H / Friedrich, Kenneth L / Mullally, James E

    EMBO reports

    2005  Volume 6, Issue 9, Page(s) 815–820

    MeSH term(s) Models, Molecular ; Peptide Hydrolases/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein Processing, Post-Translational/physiology ; Protein Structure, Tertiary ; Signal Transduction/physiology ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligase Complexes/metabolism
    Chemical Substances Ubiquitin ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; Peptide Hydrolases (EC 3.4.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2005-08-19
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 2020896-0
    ISSN 1469-3178 ; 1469-221X
    ISSN (online) 1469-3178
    ISSN 1469-221X
    DOI 10.1038/sj.embor.7400506
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: BRCA1-associated protein-1 is a tumor suppressor that requires deubiquitinating activity and nuclear localization.

    Ventii, Karen H / Devi, Narra S / Friedrich, Kenneth L / Chernova, Tatiana A / Tighiouart, Mourad / Van Meir, Erwin G / Wilkinson, Keith D

    Cancer research

    2008  Volume 68, Issue 17, Page(s) 6953–6962

    Abstract: BRCA1-associated protein-1 (BAP1), a deubiquitinating enzyme of unknown cellular function, is mutated in breast and lung cancers. In this study, we have shown for the first time that BAP1 has tumor suppressor activity in vivo by showing that BAP1 can ... ...

    Abstract BRCA1-associated protein-1 (BAP1), a deubiquitinating enzyme of unknown cellular function, is mutated in breast and lung cancers. In this study, we have shown for the first time that BAP1 has tumor suppressor activity in vivo by showing that BAP1 can suppress tumorigenicity of lung cancer cells in athymic nude mice. We show that BAP1 fulfills another criterion of a genuine tumor suppressor because cancer-associated BAP1 mutants are deficient in deubiquitinating activity. We show for the first time that one of the two predicted nuclear targeting motifs is required for nuclear localization of BAP1 and that a truncation mutant found in a lung cancer cell line results in BAP1 that fails to localize to the nucleus. Furthermore, we show that deubiquitinating activity and nuclear localization are both required for BAP1-mediated tumor suppression in nude mice. We show that BAP1 exerts its tumor suppressor functions by affecting the cell cycle, speeding the progression through the G(1)-S checkpoint, and inducing cell death via a process that has characteristics of both apoptosis and necrosis. Surprisingly, BAP1-mediated growth suppression is independent of wild-type BRCA1. Because deubiquitinating enzymes are components of the ubiquitin proteasome system, this pathway has emerged as an important target for anticancer drugs. The identification of the deubiquitinating enzyme BAP1 as a tumor suppressor may lead to further understanding of how the ubiquitin proteasome system contributes to cancer and aid in the identification of new targets for cancer therapy.
    MeSH term(s) Amino Acid Sequence ; Animals ; Cell Cycle ; Cell Division ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Female ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; Sequence Homology, Amino Acid ; Tumor Suppressor Proteins/chemistry ; Tumor Suppressor Proteins/metabolism ; Tumor Suppressor Proteins/physiology ; Ubiquitin/metabolism ; Ubiquitin Thiolesterase/chemistry ; Ubiquitin Thiolesterase/metabolism ; Ubiquitin Thiolesterase/physiology
    Chemical Substances BAP1 protein, human ; Tumor Suppressor Proteins ; Ubiquitin ; Ubiquitin Thiolesterase (EC 3.4.19.12)
    Language English
    Publishing date 2008-08-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1432-1
    ISSN 1538-7445 ; 0008-5472
    ISSN (online) 1538-7445
    ISSN 0008-5472
    DOI 10.1158/0008-5472.CAN-08-0365
    Database MEDical Literature Analysis and Retrieval System OnLINE

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