Emerging paradigm of crosstalk between autophagy and the ubiquitin-proteasome system

Taewook Nam, Jong Hyun Han, Sushil Devkota, Han Woong Lee

Research output: Contribution to journalShort survey

21 Citations (Scopus)

Abstract

Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Until recently, the UPS and autophagy were considered to be largely independent systems targeting proteins for degradation in the proteasome and lysosome, respectively. However, the identification of crucial roles of molecular players such as ubiquitin and p62 in both of these pathways as well as the observation that blocking the UPS affects autophagy flux and vice versa has generated interest in studying crosstalk between these pathways. Here, we critically review the current understanding of how the UPS and autophagy execute coordinated protein degradation at the molecular level, and shed light on our recent findings indicating an important role of an autophagy-associated transmembrane protein EI24 as a bridging molecule between the UPS and autophagy that functions by regulating the degradation of several E3 ligases with Really Interesting New Gene (RING)-domains.

Original languageEnglish
Pages (from-to)897-905
Number of pages9
JournalMolecules and cells
Volume40
Issue number12
DOIs
Publication statusPublished - 2017 Jan 1

Fingerprint

Autophagy
Proteasome Endopeptidase Complex
Ubiquitin
Proteolysis
Ubiquitin-Protein Ligases
Lysosomes
Proteins
Homeostasis
Genes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Nam, Taewook ; Han, Jong Hyun ; Devkota, Sushil ; Lee, Han Woong. / Emerging paradigm of crosstalk between autophagy and the ubiquitin-proteasome system. In: Molecules and cells. 2017 ; Vol. 40, No. 12. pp. 897-905.
@article{3c876c8afbe340a3ad27f5d61c4e5302,
title = "Emerging paradigm of crosstalk between autophagy and the ubiquitin-proteasome system",
abstract = "Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Until recently, the UPS and autophagy were considered to be largely independent systems targeting proteins for degradation in the proteasome and lysosome, respectively. However, the identification of crucial roles of molecular players such as ubiquitin and p62 in both of these pathways as well as the observation that blocking the UPS affects autophagy flux and vice versa has generated interest in studying crosstalk between these pathways. Here, we critically review the current understanding of how the UPS and autophagy execute coordinated protein degradation at the molecular level, and shed light on our recent findings indicating an important role of an autophagy-associated transmembrane protein EI24 as a bridging molecule between the UPS and autophagy that functions by regulating the degradation of several E3 ligases with Really Interesting New Gene (RING)-domains.",
author = "Taewook Nam and Han, {Jong Hyun} and Sushil Devkota and Lee, {Han Woong}",
year = "2017",
month = "1",
day = "1",
doi = "10.14348/molcells.2017.0226",
language = "English",
volume = "40",
pages = "897--905",
journal = "Molecules and Cells",
issn = "1016-8478",
publisher = "Korean Society for Molecular and Cellular Biology",
number = "12",

}

Emerging paradigm of crosstalk between autophagy and the ubiquitin-proteasome system. / Nam, Taewook; Han, Jong Hyun; Devkota, Sushil; Lee, Han Woong.

In: Molecules and cells, Vol. 40, No. 12, 01.01.2017, p. 897-905.

Research output: Contribution to journalShort survey

TY - JOUR

T1 - Emerging paradigm of crosstalk between autophagy and the ubiquitin-proteasome system

AU - Nam, Taewook

AU - Han, Jong Hyun

AU - Devkota, Sushil

AU - Lee, Han Woong

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Until recently, the UPS and autophagy were considered to be largely independent systems targeting proteins for degradation in the proteasome and lysosome, respectively. However, the identification of crucial roles of molecular players such as ubiquitin and p62 in both of these pathways as well as the observation that blocking the UPS affects autophagy flux and vice versa has generated interest in studying crosstalk between these pathways. Here, we critically review the current understanding of how the UPS and autophagy execute coordinated protein degradation at the molecular level, and shed light on our recent findings indicating an important role of an autophagy-associated transmembrane protein EI24 as a bridging molecule between the UPS and autophagy that functions by regulating the degradation of several E3 ligases with Really Interesting New Gene (RING)-domains.

AB - Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Until recently, the UPS and autophagy were considered to be largely independent systems targeting proteins for degradation in the proteasome and lysosome, respectively. However, the identification of crucial roles of molecular players such as ubiquitin and p62 in both of these pathways as well as the observation that blocking the UPS affects autophagy flux and vice versa has generated interest in studying crosstalk between these pathways. Here, we critically review the current understanding of how the UPS and autophagy execute coordinated protein degradation at the molecular level, and shed light on our recent findings indicating an important role of an autophagy-associated transmembrane protein EI24 as a bridging molecule between the UPS and autophagy that functions by regulating the degradation of several E3 ligases with Really Interesting New Gene (RING)-domains.

UR - http://www.scopus.com/inward/record.url?scp=85048166970&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85048166970&partnerID=8YFLogxK

U2 - 10.14348/molcells.2017.0226

DO - 10.14348/molcells.2017.0226

M3 - Short survey

C2 - 29237114

AN - SCOPUS:85048166970

VL - 40

SP - 897

EP - 905

JO - Molecules and Cells

JF - Molecules and Cells

SN - 1016-8478

IS - 12

ER -