HSP27 controls GATA-1 protein level during erythroid cell differentiation

Aurelie De Thonel, Julie Vandekerckhove, David Lanneau, Subramaniam Selvakumar, Geneviève Courtois, Adonis Hazoume, Mathilde Brunet, Sebastien Maurel, Arlette Hammann, Jean Antoine Ribeil, Yael Zermati, Anne Sophie Gabet, Joan Boyes, Eric Solary, Olivier Hermine, Carmen Garrido

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60 Citations (Scopus)

Résumé

Heat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34 + human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More specifically, we demonstrate that, in the late stages of the erythroid differentiation program, HSP27 is phosphorylated in a p38-dependent manner, enters the nucleus, binds to GATA-1, and induces its ubiquitination and proteasomal degradation, provided that the transcription factor is acetylated. We conclude that HSP27 plays a role in the fine-tuning of terminal erythroid differentiation through regulation of GATA-1 content and activity.

langue originaleAnglais
Pages (de - à)85-96
Nombre de pages12
journalBlood
Volume116
Numéro de publication1
Les DOIs
étatPublié - 8 juil. 2010
Modification externeOui

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