Tickets for p53 journey among organelles
Résumé
A broad range of stressors - intrinsic and extrinsic to the cell - stabilize and activate p53, affecting it by a series of post-translational modifications such as phosphorylation, acetylation, ubiquitination, methylation and sumoylation. p53 is able to integrate each kind of posttranslational modification and to adequately respond by inducing cell cycle arrest, senescence or apoptosis. p53 controls the cell fate at the level of different compartments, and its trafficking among organelles is modulated by different types of post-translational modifications. Thus, miss-location or sequestration of p53 within a compartment might obstruct its function as tumor suppressor leading to cell immortalization and tumorigenesis. The aim of this contribution is to give a unified overview of several reports in the literature, concerning the post-translational modifications endured by p53 which regulate its cellular trafficking and distribution at different organelles.
Mots clés
review
dna damage
lysosome
in-vivo
mitochondria
p53
ubiquitination
acetylation
phosphorylation
dna-damage
cytoskeleton
mdm2
nucleus
transcriptional activity
proteasome-mediated degradation
wild-type p53
transformation-related protein
nuclear-localization signal
tumor-suppressor protein
ring-finger domain
c-terminal domain
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