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The ubiquitin-proteasome system

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Abstract

The 2004 Nobel Prize in chemistry for the discovery of protein ubiquitination has led to the recognition of cellular proteolysis as a central area of research in biology. Eukaryotic proteins targeted for degradation by this pathway are first ‘tagged’ by multimers of a protein known as ubiquitin and are later proteolyzed by a giant enzyme known as the proteasome. This article recounts the key observations that led to the discovery of ubiquitin-proteasome system (UPS). In addition, different aspects of proteasome biology are highlighted. Finally, some key roles of the UPS in different areas of biology and the use of inhibitors of this pathway as possible drug targets are discussed.

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Abbreviations

AAA-ATPase:

ATPases associated with various cellular activities-ATPase

BrAAP:

branched chain amino acids preferring

CSN:

COP9 signalosome

ER:

endoplasmic reticulum

HECT:

homologous to E6-AP carboxyl terminus

IFN:

interferon

MHC:

major histocompatibility complex

NTN:

N-terminal nucleophile

PA:

proteasome activator

PAC:

proteasome assembling chaperone

PAN:

proteasome-activating nucleotidase

PI:

proteasome inhibitor

POMP:

proteasome maturing protein

RING:

really interesting new gene

Rpn:

regulatory particle non-ATPase

Rpt:

regulatory particle tripleA-ATPase

SCF:

Skp-Cullin-F box

SNAAP:

small neutral amino acids preferring

UBH:

ubiquitin hydrolase

UBP:

ubiqutin processing

UMP1:

ubiquitin mediated proteolysis-1

UPS:

ubiquitin-proteasome system

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  1. Department of Biochemistry, Indian Institute of Science, 560 012, Bangalore, India

    Dipankar Nandi, Pankaj Tahiliani, Anujith Kumar & Dilip Chandu

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Nandi, D., Tahiliani, P., Kumar, A. et al. The ubiquitin-proteasome system. J. Biosci. 31, 137–155 (2006). https://doi.org/10.1007/BF02705243

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