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The Biogenesis of the Eukaryotic Proteasome

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The Molecular Chaperones Interaction Networks in Protein Folding and Degradation

Part of the book series: Interactomics and Systems Biology ((INTERACTOM,volume 1))

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Abstract

Proteasomes are at the heart of the ubiquitin-proteasome system and are responsible for the degradation of the majority of intracellular proteins in eukaryotes. Consequently, proteasome activity impacts all cellular processes. Recent structural advances have provided the most informative view yet of the architecture of the proteasome, enriching our already detailed knowledge of its function. An interesting question, which continues to draw much experimental attention, is how these large molecular machines are put together in the first place. Over the last decade, the picture that has emerged is that of an ordered, efficient, and highly regulated process. Assembly of the proteasome is dependent upon intrinsic structural features distributed among the ~ 33 subunits that comprise it, and upon extrinsic protein factors, some of which function as dedicated proteasome chaperones. This chapter summarizes our understanding of the mechanism by which cells bring proteasomes into existence.

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Abbreviations

UPS:

Ubiquitin proteasome system

CP:

Core particle

RP:

Regulatory particle

Rpt:

Regulatory particle ATPase

Rpn:

Regulatory particle non-ATPase

HbYX:

Hydrophobic-tyrosine-any amino acid

PHP:

Preholoproteasome

ER:

Endoplasmic reticulum

PAC:

Proteasome assembly chaperone

RAC:

RP assembly chaperone

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  1. Department of Biology, Indiana University-Purdue University Indianapolis, 723 West Michigan Street, 46202, Indianapolis, IN, USA

    Andrew R. Kusmierczyk

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    Walid A. Houry

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Kusmierczyk, A. (2014). The Biogenesis of the Eukaryotic Proteasome. In: Houry, W. (eds) The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Interactomics and Systems Biology, vol 1. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1130-1_13

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