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

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

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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",

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