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The interaction of the von Hippel-Lindau tumor suppressor and heterochromatin protein 1.

Abstract：

:Inactivation of the von Hippel-Lindau (VHL) tumor suppressor is associated with renal carcinoma, hemangioblastoma and pheochromocytoma. The VHL protein is a component of a ubiquitin ligase complex that ubiquitinates and degrades hypoxia inducible factor-α (HIF-α). Degradation of HIF-α by VHL is proposed to suppress tumorigenesis and tumor angiogenesis. Several lines of evidence also suggest important roles for HIF-independent VHL functions in tumor suppression and other biological processes. Using GST-VHL pull-down experiment and mass spectrometry, we detected an interaction between VHL and heterochromatin protein 1 (HP1). We identified a conserved HP1-binding motif (PXVXL) in the β domain of VHL, which is disrupted in a renal carcinoma-associated P81S mutant. We show that the VHL P81S mutant displays reduced binding to HP1, yet retains the ability to interact with elongin B, elongin C, and cullin 2 and is fully capable of degrading HIF-α. We also demonstrate that HP1 increases the chromatin association of VHL. These results suggest a role for the VHL-HP1 interaction in VHL chromatin targeting.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Lai Y,Song M,Hakala K,Weintraub ST,Shiio Y

doi

10.1016/j.abb.2011.12.023

subject

Has Abstract

pub_date

2012-02-15 00:00:00

pages

103-10

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(11)00435-8

journal_volume

518

pub_type

杂志文章

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