Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains

Han Seok Ko, Takashi Uehara, Kazuhiro Tsuruma, Yasuyuki Nomura

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.

Original languageEnglish
Pages (from-to)110-114
Number of pages5
JournalFEBS Letters
Volume566
Issue number1-3
DOIs
Publication statusPublished - May 21 2004
Externally publishedYes

Fingerprint

Protein Disulfide-Isomerases
Proteasome Endopeptidase Complex
Ubiquitin
Polyubiquitin
Brain Hypoxia-Ischemia
Endoplasmic Reticulum
Cytosol
Brain
Proteins
Genes
Cells
Membranes

Keywords

  • ER, endoplasmic reticulum
  • ERAD, ER-associated degradation
  • NP, asparagine-proline repeats
  • Ub, ubiquitin
  • UBA, ubiquitin-associated
  • UBA52, ubiquitin amino acid 52-residue ribosomal protein fusion
  • UBL, ubiquitin-like
  • UPR, unfolded protein response

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains. / Ko, Han Seok; Uehara, Takashi; Tsuruma, Kazuhiro; Nomura, Yasuyuki.

In: FEBS Letters, Vol. 566, No. 1-3, 21.05.2004, p. 110-114.

Research output: Contribution to journalArticle

@article{74983ce779f9480db949051b9a234109,
title = "Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains",
abstract = "Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.",
keywords = "ER, endoplasmic reticulum, ERAD, ER-associated degradation, NP, asparagine-proline repeats, Ub, ubiquitin, UBA, ubiquitin-associated, UBA52, ubiquitin amino acid 52-residue ribosomal protein fusion, UBL, ubiquitin-like, UPR, unfolded protein response",
author = "Ko, {Han Seok} and Takashi Uehara and Kazuhiro Tsuruma and Yasuyuki Nomura",
year = "2004",
month = "5",
day = "21",
doi = "10.1016/j.febslet.2004.04.031",
language = "English",
volume = "566",
pages = "110--114",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1-3",

}

TY - JOUR

T1 - Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains

AU - Ko, Han Seok

AU - Uehara, Takashi

AU - Tsuruma, Kazuhiro

AU - Nomura, Yasuyuki

PY - 2004/5/21

Y1 - 2004/5/21

N2 - Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.

AB - Mammalian cells acquire tolerance against multiple stressors through the high-level expression of stress-responsible genes. We have previously demonstrated that protein-disulfide isomerase (PDI) together with ubiquilin are up-regulated in response to hypoxia/brain ischemia, and play critical roles in resistance to these damages. We show here that ubiquilin interacts preferentially with poly-ubiquitin chains and 19S proteasome subunits. Taken together, these results suggest that ubiquitin could serve as an adaptor protein that both interacts with PDI and mediates the delivery of poly-ubiquitylated proteins to the proteasome in the cytosol in the vicinity of the endoplasmic reticulum membrane.

KW - ER, endoplasmic reticulum

KW - ERAD, ER-associated degradation

KW - NP, asparagine-proline repeats

KW - Ub, ubiquitin

KW - UBA, ubiquitin-associated

KW - UBA52, ubiquitin amino acid 52-residue ribosomal protein fusion

KW - UBL, ubiquitin-like

KW - UPR, unfolded protein response

UR - http://www.scopus.com/inward/record.url?scp=2442520399&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2442520399&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2004.04.031

DO - 10.1016/j.febslet.2004.04.031

M3 - Article

C2 - 15147878

AN - SCOPUS:2442520399

VL - 566

SP - 110

EP - 114

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1-3

ER -