Proposed model for the coordinated molecular events that may control GATA-1 level and erythroblast differentiation. Activation of p38MAPK during erythropoiesis was described previously to promote GATA-1 phosphorylation and acetylation²⁸  and to phosphorylate HSP27 through MAPKAPK2 activation.^26,28  The present study indicates that phosphorylated HSP27 accumulates in the nucleus and interacts with GATA-1 to induce its ubiquitination and proteasomal degradation. GATA-1 acetylation precedes its degradation by the proteasomal machinery. This model provides new evidence of the major role of chaperones in erythropoiesis.²⁹  **Reference to data from the literature as mentioned above.