Integration of clearance mechanisms

the proteasome and autophagy.

Esther Wong, Ana Maria Cuervo

Research output: Contribution to journalArticle

177 Citations (Scopus)

Abstract

Cells maintain a healthy proteome through continuous evaluation of the quality of each of their proteins. Quality control requires the coordinated action of chaperones and proteolytic systems. Chaperones identify abnormal or unstable conformations in proteins and often assist them to regain stability. However, if repair is not possible, the aberrant protein is eliminated from the cellular cytosol to prevent undesired interactions with other proteins or its organization into toxic multimeric complexes. Autophagy and the ubiquitin/proteasome system mediate the complete degradation of abnormal protein products. In this article, we describe each of these proteolytic systems and their contribution to cellular quality control. We also comment on the cellular consequences resulting from the dysfunction of these systems in common human protein conformational disorders and provide an overview on current therapeutic interventions based on the modulation of the proteolytic systems.

Original languageEnglish (US)
JournalCold Spring Harbor perspectives in biology
Volume2
Issue number12
StatePublished - Dec 1 2010
Externally publishedYes

Fingerprint

Autophagy
Proteasome Endopeptidase Complex
Quality Control
Proteins
Protein Conformation
Quality control
Poisons
Proteome
Ubiquitin
Cytosol
Proteolysis
Regain
Conformations
Repair
Modulation
Degradation
Therapeutics

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Integration of clearance mechanisms : the proteasome and autophagy. / Wong, Esther; Cuervo, Ana Maria.

In: Cold Spring Harbor perspectives in biology, Vol. 2, No. 12, 01.12.2010.

Research output: Contribution to journalArticle

@article{0a20ae4bb78d46a1b5171206141488cf,
title = "Integration of clearance mechanisms: the proteasome and autophagy.",
abstract = "Cells maintain a healthy proteome through continuous evaluation of the quality of each of their proteins. Quality control requires the coordinated action of chaperones and proteolytic systems. Chaperones identify abnormal or unstable conformations in proteins and often assist them to regain stability. However, if repair is not possible, the aberrant protein is eliminated from the cellular cytosol to prevent undesired interactions with other proteins or its organization into toxic multimeric complexes. Autophagy and the ubiquitin/proteasome system mediate the complete degradation of abnormal protein products. In this article, we describe each of these proteolytic systems and their contribution to cellular quality control. We also comment on the cellular consequences resulting from the dysfunction of these systems in common human protein conformational disorders and provide an overview on current therapeutic interventions based on the modulation of the proteolytic systems.",
author = "Esther Wong and Cuervo, {Ana Maria}",
year = "2010",
month = "12",
day = "1",
language = "English (US)",
volume = "2",
journal = "Cold Spring Harbor perspectives in biology",
issn = "1943-0264",
publisher = "Cold Spring Harbor Laboratory Press",
number = "12",

}

TY - JOUR

T1 - Integration of clearance mechanisms

T2 - the proteasome and autophagy.

AU - Wong, Esther

AU - Cuervo, Ana Maria

PY - 2010/12/1

Y1 - 2010/12/1

N2 - Cells maintain a healthy proteome through continuous evaluation of the quality of each of their proteins. Quality control requires the coordinated action of chaperones and proteolytic systems. Chaperones identify abnormal or unstable conformations in proteins and often assist them to regain stability. However, if repair is not possible, the aberrant protein is eliminated from the cellular cytosol to prevent undesired interactions with other proteins or its organization into toxic multimeric complexes. Autophagy and the ubiquitin/proteasome system mediate the complete degradation of abnormal protein products. In this article, we describe each of these proteolytic systems and their contribution to cellular quality control. We also comment on the cellular consequences resulting from the dysfunction of these systems in common human protein conformational disorders and provide an overview on current therapeutic interventions based on the modulation of the proteolytic systems.

AB - Cells maintain a healthy proteome through continuous evaluation of the quality of each of their proteins. Quality control requires the coordinated action of chaperones and proteolytic systems. Chaperones identify abnormal or unstable conformations in proteins and often assist them to regain stability. However, if repair is not possible, the aberrant protein is eliminated from the cellular cytosol to prevent undesired interactions with other proteins or its organization into toxic multimeric complexes. Autophagy and the ubiquitin/proteasome system mediate the complete degradation of abnormal protein products. In this article, we describe each of these proteolytic systems and their contribution to cellular quality control. We also comment on the cellular consequences resulting from the dysfunction of these systems in common human protein conformational disorders and provide an overview on current therapeutic interventions based on the modulation of the proteolytic systems.

UR - http://www.scopus.com/inward/record.url?scp=79952585579&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79952585579&partnerID=8YFLogxK

M3 - Article

VL - 2

JO - Cold Spring Harbor perspectives in biology

JF - Cold Spring Harbor perspectives in biology

SN - 1943-0264

IS - 12

ER -