Proteasome activators

Beth M. Stadtmueller, Christopher P. Hill

Research output: Contribution to journalReview article

Abstract

Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access. Structural and biochemical studies of two activator families, 11S and Blm10, have provided insights to proteasome activation mechanisms, although the biological functions of these factors remain obscure. Recent advances have improved our understanding of the third activator family, including the 19S activator, which targets polyubiquitylated proteins for degradation. Here we present a structural perspective on how proteasomes are activated and how substrates are delivered to the proteolytic sites.

Original languageEnglish (US)
Pages (from-to)8-19
Number of pages12
JournalMolecular cell
Volume41
Issue number1
DOIs
StatePublished - Jan 7 2011
Externally publishedYes

Fingerprint

Proteasome Endopeptidase Complex
Biological Factors
Cytosol
Proteolysis
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Proteasome activators. / Stadtmueller, Beth M.; Hill, Christopher P.

In: Molecular cell, Vol. 41, No. 1, 07.01.2011, p. 8-19.

Research output: Contribution to journalReview article

Stadtmueller, Beth M. ; Hill, Christopher P. / Proteasome activators. In: Molecular cell. 2011 ; Vol. 41, No. 1. pp. 8-19.
@article{9cb6e7528c5844239f470672ca903095,
title = "Proteasome activators",
abstract = "Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access. Structural and biochemical studies of two activator families, 11S and Blm10, have provided insights to proteasome activation mechanisms, although the biological functions of these factors remain obscure. Recent advances have improved our understanding of the third activator family, including the 19S activator, which targets polyubiquitylated proteins for degradation. Here we present a structural perspective on how proteasomes are activated and how substrates are delivered to the proteolytic sites.",
author = "Stadtmueller, {Beth M.} and Hill, {Christopher P.}",
year = "2011",
month = "1",
day = "7",
doi = "10.1016/j.molcel.2010.12.020",
language = "English (US)",
volume = "41",
pages = "8--19",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "1",

}

TY - JOUR

T1 - Proteasome activators

AU - Stadtmueller, Beth M.

AU - Hill, Christopher P.

PY - 2011/1/7

Y1 - 2011/1/7

N2 - Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access. Structural and biochemical studies of two activator families, 11S and Blm10, have provided insights to proteasome activation mechanisms, although the biological functions of these factors remain obscure. Recent advances have improved our understanding of the third activator family, including the 19S activator, which targets polyubiquitylated proteins for degradation. Here we present a structural perspective on how proteasomes are activated and how substrates are delivered to the proteolytic sites.

AB - Proteasomes degrade a multitude of protein substrates in the cytosol and nucleus, and thereby are essential for many aspects of cellular function. Because the proteolytic sites are sequestered in a closed barrel-shaped structure, activators are required to facilitate substrate access. Structural and biochemical studies of two activator families, 11S and Blm10, have provided insights to proteasome activation mechanisms, although the biological functions of these factors remain obscure. Recent advances have improved our understanding of the third activator family, including the 19S activator, which targets polyubiquitylated proteins for degradation. Here we present a structural perspective on how proteasomes are activated and how substrates are delivered to the proteolytic sites.

UR - http://www.scopus.com/inward/record.url?scp=78650720758&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78650720758&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2010.12.020

DO - 10.1016/j.molcel.2010.12.020

M3 - Review article

C2 - 21211719

AN - SCOPUS:78650720758

VL - 41

SP - 8

EP - 19

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 1

ER -