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Oncogene. 2010 Jan 21;29(3):403-10. doi: 10.1038/onc.2009.321. Epub 2009 Oct 19.

Genotoxic stress-induced nuclear localization of oncoprotein YB-1 in the absence of proteolytic processing.

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1
Cell Transformation Unit, Children's Medical Research Institute, Westmead, New South Wales, 2145, Australia.

Abstract

Y-box-binding protein 1 (YB-1) is an oncogenic transcription factor whose overexpression and nuclear localization is associated with tumor progression and drug resistance. Transcriptional activation of YB-1 in response to genotoxic stress is believed to occur in the cytoplasm through sequence-specific endoproteolytic cleavage by the 20S Proteasome, followed by nuclear translocation of cleaved YB-1. To study the proteolysis model, we developed a two-step affinity purification of endogenous YB-1 protein species and characterized the products using mass spectrometry. Whereas full-length YB-1 was readily identified, the smaller protein band thought to be activated YB-1 was identified as hnRNP A1. An antibody specific for YB-1 was generated, which revealed only one YB-1 species, even after genotoxic stress-induced nuclear YB-1 translocation. These findings warrant re-evaluation of the mechanism of YB-1 nuclear translocation and transcriptional activation. The relationship between nuclear YB-1 and tumor progression may also have to re-evaluated in some cases.

PMID:
19838214
DOI:
10.1038/onc.2009.321
[Indexed for MEDLINE]
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