The von Hippel–Lindau tumour suppressor protein: O2 sensing and cancer

2008 ◽  
Vol 8 (11) ◽  
pp. 865-873 ◽  
Author(s):  
William G. Kaelin Jr
Keyword(s):  
Tumour Suppressor ◽  
Von Hippel Lindau ◽  
Tumour Suppressor Protein ◽  
O2 Sensing

scholarly journals Functions of the von Hippel–Lindau tumour suppressor protein

1998 ◽  
Vol 243 (6) ◽  
pp. 535-539 ◽  
Author(s):  
Kaelin ◽  
Iliopoulos ◽  
Lonergan ◽  
Ohh
Keyword(s):  
Tumour Suppressor ◽  
Von Hippel Lindau ◽  
Tumour Suppressor Protein

The multifaceted von Hippel-Lindau tumour suppressor protein

FEBS Letters ◽  
2014 ◽  
Vol 588 (16) ◽  
pp. 2704-2711 ◽  
Author(s):  
Claire M. Robinson ◽  
Michael Ohh
Keyword(s):  
Tumour Suppressor ◽  
Von Hippel Lindau ◽  
Tumour Suppressor Protein

Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL

2002 ◽  
Vol 5 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Alexander Hergovich ◽  
Joanna Lisztwan ◽  
Robert Barry ◽  
Pia Ballschmieter ◽  
Wilhelm Krek
Keyword(s):  
Tumour Suppressor ◽  
Von Hippel Lindau ◽  
Microtubule Stability ◽  
Tumour Suppressor Protein

scholarly journals The von Hippel–Lindau tumour-suppressor protein interaction with protein kinase Cδ

2006 ◽  
Vol 397 (1) ◽  
pp. 109-120 ◽  
Author(s):  
Xavier Iturrioz ◽  
Joanne Durgan ◽  
Véronique Calleja ◽  
Banafshé Larijani ◽  
Heiwa Okuda ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Ubiquitin Ligase ◽  
Catalytic Domain ◽  
Interaction Analysis ◽  
Resonance Energy ◽  
Tumour Suppressor ◽  
Fluorescence Lifetime Imaging ◽  
Α Subunit ◽  
Von Hippel Lindau ◽  
Tumour Suppressor Protein

The VHL (von Hippel–Lindau) tumour-suppressor protein forms a multi-protein complex [VCB (pVHL–elongin C–elongin B)–Cul-2 (Cullin-2)] with elongin C, elongin B, Cul-2 and Rbx1, acting as a ubiquitin-ligase (E3) and directing proteasome-dependent degradation of targeted proteins. The α-subunit of Hif1α (hypoxia-inducible factor 1α) is the principal substrate for the VCB–Cul-2 complex; however, other substrates such as aPKC (atypical protein kinase C) have been reported. In the present study, we show with FRET (fluorescence resonance energy transfer) analysis measured by FLIM (fluorescence lifetime imaging microscopy) that PKCδ and pVHL (VHL protein) interact directly in cells. This occurs through the catalytic domain of PKCδ (residues 432–508), which appears to interact with two regions of pVHL, residues 113–122 and 130–154. Despite this robust interaction, analysis of the PMA-induced proteasome-dependent degradation of PKCδ in different RCC (renal cell carcinoma) lines (RCC4, UMRC2 and 786 O) shows that there is no correlation between the degradation of PKCδ and the presence of active pVHL. Thus, in contrast with aPKC, PKCδ is not a conventional substrate of the ubiquitin-ligase complex, VCB–Cul-2, and the observed interaction between these two proteins must underlie a distinct signalling output.

Mobility of the von Hippel–Lindau tumour suppressor protein is regulated by kinesin-2

2008 ◽  
Vol 314 (6) ◽  
pp. 1229-1236 ◽  
Author(s):  
Dorus A. Mans ◽  
Martijn P. Lolkema ◽  
Moniek van Beest ◽  
Laura G. Daenen ◽  
Emile E. Voest ◽  
...  
Keyword(s):  
Tumour Suppressor ◽  
Von Hippel Lindau ◽  
Tumour Suppressor Protein

Regulation of E2F1 by the von Hippel-Lindau tumour suppressor protein predicts survival in renal cell cancer patients

2013 ◽  
Vol 231 (1) ◽  
pp. 117-129 ◽  
Author(s):  
Dorus A Mans ◽  
Joost S Vermaat ◽  
Bart G Weijts ◽  
Ellen van Rooijen ◽  
Jeroen van Reeuwijk ◽  
...  
Keyword(s):  
Cancer Patients ◽  
Renal Cell Cancer ◽  
Renal Cell ◽  
Cell Cancer ◽  
Tumour Suppressor ◽  
Von Hippel Lindau ◽  
Tumour Suppressor Protein
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