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PLoS One. 2011 Feb 28;6(2):e16975. doi: 10.1371/journal.pone.0016975.

Quantitative proteomics identifies the Myb-binding protein p160 as a novel target of the von Hippel-Lindau tumor suppressor.

Author information

1
Greehey Children's Cancer Research Institute, San Antonio, Texas, United States of America.

Abstract

BACKGROUND:

The von Hippel-Lindau (VHL) tumor suppressor gene encodes a component of a ubiquitin ligase complex, which is best understood as a negative regulator of hypoxia inducible factor (HIF). VHL ubiquitinates and degrades the α subunits of HIF, and this is proposed to suppress tumorigenesis and tumor angiogenesis. However, several lines of evidence suggest that there are unidentified substrates or targets for VHL that play important roles in tumor suppression.

METHODOLOGY/PRINCIPAL FINDINGS:

Employing quantitative proteomics, we developed an approach to systematically identify the substrates of ubiquitin ligases and using this method, we identified the Myb-binding protein p160 as a novel substrate of VHL.

CONCLUSIONS/SIGNIFICANCE:

A major barrier to understanding the functions of ubiquitin ligases has been the difficulty in pinpointing their ubiquitination substrates. The quantitative proteomics approach we devised for the identification of VHL substrates will be widely applicable to other ubiquitin ligases.

PMID:
21386990
PMCID:
PMC3046137
DOI:
10.1371/journal.pone.0016975
[Indexed for MEDLINE]
Free PMC Article

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