Deubiquitylating enzymes and disease

Shweta Singhal; Matthew C. Taylor; Rohan T. Baker

doi:10.1186/1471-2091-9-S1-S3

Deubiquitylating enzymes and disease

Shweta Singhal, Matthew C. Taylor, Rohan T. Baker

Research output: Contribution to journal › Review article › peer-review

74 Citations (Scopus)

Abstract

Deubiquitylating enzymes (DUBs) can hydrolyze a peptide, amide, ester or thiolester bond at the C-terminus of UBIQ (ubiquitin), including the post-translationally formed branched peptide bonds in mono- or multi-ubiquitylated conjugates. DUBs thus have the potential to regulate any UBIQ-mediated cellular process, the two best characterized being proteolysis and protein trafficking. Mammals contain some 80-90 DUBs in five different subfamilies, only a handful of which have been characterized with respect to the proteins that they interact with and deubiquitylate. Several other DUBs have been implicated in various disease processes in which they are changed by mutation, have altered expression levels, and/or form part of regulatory complexes. Specific examples of DUB involvement in various diseases are presented. While no specific drugs targeting DUBs have yet been described, sufficient functional and structural information has accumulated in some cases to allow their rapid development. Publication history. Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com).

Original language	English
Article number	S3
Journal	BMC Biochemistry
Volume	9
Issue number	SUPPL. 1
DOIs	https://doi.org/10.1186/1471-2091-9-S1-S3
Publication status	Published - 2008

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title = "Deubiquitylating enzymes and disease",

abstract = "Deubiquitylating enzymes (DUBs) can hydrolyze a peptide, amide, ester or thiolester bond at the C-terminus of UBIQ (ubiquitin), including the post-translationally formed branched peptide bonds in mono- or multi-ubiquitylated conjugates. DUBs thus have the potential to regulate any UBIQ-mediated cellular process, the two best characterized being proteolysis and protein trafficking. Mammals contain some 80-90 DUBs in five different subfamilies, only a handful of which have been characterized with respect to the proteins that they interact with and deubiquitylate. Several other DUBs have been implicated in various disease processes in which they are changed by mutation, have altered expression levels, and/or form part of regulatory complexes. Specific examples of DUB involvement in various diseases are presented. While no specific drugs targeting DUBs have yet been described, sufficient functional and structural information has accumulated in some cases to allow their rapid development. Publication history. Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com).",

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T1 - Deubiquitylating enzymes and disease

AU - Singhal, Shweta

AU - Taylor, Matthew C.

AU - Baker, Rohan T.

PY - 2008

Y1 - 2008

N2 - Deubiquitylating enzymes (DUBs) can hydrolyze a peptide, amide, ester or thiolester bond at the C-terminus of UBIQ (ubiquitin), including the post-translationally formed branched peptide bonds in mono- or multi-ubiquitylated conjugates. DUBs thus have the potential to regulate any UBIQ-mediated cellular process, the two best characterized being proteolysis and protein trafficking. Mammals contain some 80-90 DUBs in five different subfamilies, only a handful of which have been characterized with respect to the proteins that they interact with and deubiquitylate. Several other DUBs have been implicated in various disease processes in which they are changed by mutation, have altered expression levels, and/or form part of regulatory complexes. Specific examples of DUB involvement in various diseases are presented. While no specific drugs targeting DUBs have yet been described, sufficient functional and structural information has accumulated in some cases to allow their rapid development. Publication history. Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com).

AB - Deubiquitylating enzymes (DUBs) can hydrolyze a peptide, amide, ester or thiolester bond at the C-terminus of UBIQ (ubiquitin), including the post-translationally formed branched peptide bonds in mono- or multi-ubiquitylated conjugates. DUBs thus have the potential to regulate any UBIQ-mediated cellular process, the two best characterized being proteolysis and protein trafficking. Mammals contain some 80-90 DUBs in five different subfamilies, only a handful of which have been characterized with respect to the proteins that they interact with and deubiquitylate. Several other DUBs have been implicated in various disease processes in which they are changed by mutation, have altered expression levels, and/or form part of regulatory complexes. Specific examples of DUB involvement in various diseases are presented. While no specific drugs targeting DUBs have yet been described, sufficient functional and structural information has accumulated in some cases to allow their rapid development. Publication history. Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com).

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U2 - 10.1186/1471-2091-9-S1-S3

DO - 10.1186/1471-2091-9-S1-S3

M3 - Review article

SN - 1471-2091

VL - 9

JO - BMC Biochemistry

JF - BMC Biochemistry

IS - SUPPL. 1

M1 - S3

ER -

Deubiquitylating enzymes and disease

Abstract

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