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

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

doi:10.1016/j.febslet.2004.04.031

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 journal › Article › peer-review

128 Scopus citations

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 language	English (US)
Pages (from-to)	110-114
Number of pages	5
Journal	FEBS Letters
Volume	566
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.04.031
State	Published - May 21 2004
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2004.04.031

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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, UBA, ubiquitin-associated, UBA52, ubiquitin amino acid 52-residue ribosomal protein fusion, UBL, ubiquitin-like, UPR, unfolded protein response, Ub, ubiquitin",

author = "Ko, {Han Seok} and Takashi Uehara and Kazuhiro Tsuruma and Yasuyuki Nomura",

note = "Funding Information: We thank Dr. Keiji Tanaka (Tokyo Metropolitan Institute of Medical Science), Dr. Hiroyuki Kawahara, and Prof. Hideyoshi Yokosawa (Hokkaido University) for the provision of plasmids and their helpful discussions. This work was supported by a Grant-in-Aid from the Ministry of Education, Science, and Sports of Japan.",

year = "2004",

month = may,

day = "21",

doi = "10.1016/j.febslet.2004.04.031",

language = "English (US)",

volume = "566",

pages = "110--114",

journal = "FEBS Letters",

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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

N1 - Funding Information: We thank Dr. Keiji Tanaka (Tokyo Metropolitan Institute of Medical Science), Dr. Hiroyuki Kawahara, and Prof. Hideyoshi Yokosawa (Hokkaido University) for the provision of plasmids and their helpful discussions. This work was supported by a Grant-in-Aid from the Ministry of Education, Science, and Sports of Japan.

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 - UBA, ubiquitin-associated

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

KW - UBL, ubiquitin-like

KW - UPR, unfolded protein response

KW - Ub, ubiquitin

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SN - 0014-5793

VL - 566

SP - 110

EP - 114

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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