Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway

Xin Bao; Jill L. Johnson; Hai Rao

doi:10.1074/jbc.M114.618793

Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway

Xin Bao, Jill L. Johnson, Hai Rao

Molecular Medicine

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

Abstract

Background: The proteolytic regulation of DNA repair factors remains poorly understood. Results: Six proteins involved in nucleotide excision repair are found to be degraded by the proteasome. Conclusion: Rad25 is selected for proteasomal degradation by the Ubc4-Ufd4 pathway. Significance: Our results provide novel insights into the role of the proteasome in DNA repair.

Original language	English (US)
Pages (from-to)	8606-8612
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	290
Issue number	13
DOIs	https://doi.org/10.1074/jbc.M114.618793
State	Published - Mar 27 2015

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1074/jbc.M114.618793

Fingerprint Dive into the research topics of 'Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway'. Together they form a unique fingerprint.

Cite this

@article{b976c1ef02724d95adec1a7702c9ac59,

title = "Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway",

abstract = "Background: The proteolytic regulation of DNA repair factors remains poorly understood. Results: Six proteins involved in nucleotide excision repair are found to be degraded by the proteasome. Conclusion: Rad25 is selected for proteasomal degradation by the Ubc4-Ufd4 pathway. Significance: Our results provide novel insights into the role of the proteasome in DNA repair.",

author = "Xin Bao and Johnson, {Jill L.} and Hai Rao",

year = "2015",

month = mar,

day = "27",

doi = "10.1074/jbc.M114.618793",

language = "English (US)",

volume = "290",

pages = "8606--8612",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "13",

}

TY - JOUR

T1 - Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway

AU - Bao, Xin

AU - Johnson, Jill L.

AU - Rao, Hai

PY - 2015/3/27

Y1 - 2015/3/27

N2 - Background: The proteolytic regulation of DNA repair factors remains poorly understood. Results: Six proteins involved in nucleotide excision repair are found to be degraded by the proteasome. Conclusion: Rad25 is selected for proteasomal degradation by the Ubc4-Ufd4 pathway. Significance: Our results provide novel insights into the role of the proteasome in DNA repair.

AB - Background: The proteolytic regulation of DNA repair factors remains poorly understood. Results: Six proteins involved in nucleotide excision repair are found to be degraded by the proteasome. Conclusion: Rad25 is selected for proteasomal degradation by the Ubc4-Ufd4 pathway. Significance: Our results provide novel insights into the role of the proteasome in DNA repair.

UR - http://www.scopus.com/inward/record.url?scp=84925764017&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84925764017&partnerID=8YFLogxK

U2 - 10.1074/jbc.M114.618793

DO - 10.1074/jbc.M114.618793

M3 - Article

C2 - 25670855

AN - SCOPUS:84925764017

VL - 290

SP - 8606

EP - 8612

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 13

ER -

Rad25 protein is targeted for degradation by the Ubc4-Ufd4 pathway

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this