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cAMP response element binding protein (CREB) is a transcription factor in nucleus. The activating CREB can specifically bind to the cAMP response element (CRE). The present result showed that erythropoietin (EPO) could induce the phosphorylation of CREB on Serine133(Pser133), as detected by Western blot analysis. In addition, the EPO-dependent activation of CREB binding to CRE element was demonstrated by electrophoretic mobility shift assay. However, the binding of CREB to CRE element could be inhibited by anti-CREB-Pser133antibody. The data obtained suggested that the EPO-mediated CREB phosphorylation might be critical to both the binding of CREB to the CRE element and the activation of the CREB transcription factor.