VHL which promotes HIF-1α ubiquitination and its subsequent proteasomal degradation ❋ Daniela Trisciuoglio Et Al. (2010)
To further assess the stability of PINK1 under depolarizing conditions, we performed the same set of experiments in the presence of MG132, an inhibitor of proteasomal degradation. ❋ Derek P. Narendra Et Al. (2010)
By dissecting the molecular mechanism of this process, we found that bcl-2 increases HIF-1α protein stability through the involvement of the molecular chaperone HSP90, which was found to protect HIF-1α from proteasomal degradation, even in VHL-deficient cells ❋ Daniela Trisciuoglio Et Al. (2010)
Elimination of disulfide bonds in murine Proinsulin 2, in bovine viral diarrhea virus E2 glycoproteins as well as in Human ABCG2 render these proteins sensitive to proteasomal degradation. ❋ Virginie Renaud Et Al. (2010)
Candidate must also have strong technical and conceptual background related to analysis of proteasomal and lysosomal functions, and experience with mouse model for breast and ovarian cancer. ❋ Unknown (2010)
KRP1 is regulated both transcriptionally and post-translationally through regulation of nuclear localization and through proteasomal degradation ❋ Adrienne H. K. Roeder Et Al. (2010)
Isolated PA28-αβ stimulated proteasomal activity on Suc-LLVY-MCA substrate up to five-fold and no activity was observed in controls without 20S proteasome testifying the absence of protease contamination in the PA28-αβ preparation. ❋ Michele Mishto Et Al. (2010)
PHDs-mediated hydroxylation targets HIF-1α for proteasomal degradation via the ubiquitination-dependent Von Hippel-Lindau (VHL) complex, while FIH-1-mediated hydroxylation leads to the inhibition of HIF-1 transactivation. ❋ Daniela Trisciuoglio Et Al. (2010)
The regulation of HIF-1α stability by an oxygen-independent degradation pathway was also reported: the molecular chaperone Heat Shock Protein 90 (HSP90) binds and stabilizes HIF-1α, competing with Receptor of Activated protein Kinase C (RACK1), which mediates prolyl hydroxylase/VHL-independent ubiquitination and proteasomal degradation of HIF-1α ❋ Daniela Trisciuoglio Et Al. (2010)
In conclusion, our study establishes a molecular link and highlights the possibility that bcl-2 is a new HIF-1α-binding protein whose multivalent interactions are required for the stabilization of HIF-1α, and that nuclear localization of bcl-2 may have an important role in protecting HIF-1α from ubiquitination and proteasomal degradation that commences in the nucleus. ❋ Daniela Trisciuoglio Et Al. (2010)
A recent report demonstrated that RACK1 protein promotes ubiquitination of HIF-1α induced by the HSP90 inhibitor 17-AAG and its subsequent VHL-independent proteasomal degradation competing with HSP90 for binding to PAS domain of HIF-1α ❋ Daniela Trisciuoglio Et Al. (2010)
A recent study found that a mouse model of chronically reduced proteasomal activity in the brain showed elevated concentrations of several proteins, some of which had previously been found to alter expression in the brain in Alzheimer's disease ❋ Nicholas A. Bishop (2010)
However, it has not been fully established whether proteasomal degradation of HIF-1α occurs in the nucleus, in the cytoplasm, or if it can take place in both compartments. ❋ Unknown (2009)
It has been proposed, that interaction between pVHL and HIF-1α occurs in the nucleus, where HIF-1α protein is ubiquitinated and then exported to the cytoplasm for further proteasomal degradation ❋ Unknown (2009)
It has been shown that aminopeptidases in the endoplasmic reticulum that process antigenic precursors generated by proteasomal degradation, thus generating peptides suitable for presentation by MHC class I molecules, fail to trim prolines that flank the NH2-termini of these precursors ❋ Jacqueline Schmuckli-Maurer Et Al. (2009)
During hypoxia, however, inactivation of the prolyl-hydroxylases occurs, resulting in the stabilisation of HIF-α on account proteasomal degradation of the subunit being inhibited. ❋ Unknown (2009)
This hydroxylation allows the HIF-α to bind to an ubiquitin ligase complex, the process of polyubiquination, which in turn labels it for proteasomal degradation. ❋ Unknown (2009)
Roux D, Richard DE, Pouyssegur J (2001) Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O (2) - driven proteasomal degradation irrespective of its subcellular localization: nucleus or cytoplasm. ❋ Unknown (2009)
HIF-1α protein is constantly modified posttranslationally by prolyl hydroxylases at Pro402 and / or Pro564 within the oxygen-dependent degradation (ODD) domain which promotes binding with pVHL (von Hippel-Lindau protein) and subsequent targeting for rapid proteasomal degradation. ❋ Unknown (2009)
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