Endothelial cell migration is required in the physiological angiogenic process, but also contributes to various pathological conditions, including tumor vascularization. Protein phosphatase 1 (PP1) is the major serine/threonine specific protein phosphatase and the expression of PP1cB, the beta isoform of the catalytic subunit of PP1, has been shown to be upregulated in certain cancers, as well as in chronic hypoxia, one of the major regulator in angiogenesis.The finding that PP1cB is overexpressed in several cancers, and that angiogenesis is a hallmark of cancer development, with certain tumors developing a hypoxic microenvironment to further potentiate its vascularization and growth, suggest that PP1cB might play an essential role in angiogenesis. Hence, the potential role of PP1cB in angiogenesis is investigated in the present study.The effect of knocking down and overexpressing PP1cB on endothelial cell migration and endothelial morphogenesis was examined using in vitro wound healing scratch assay and in vitro endothelial tube formation assay respectively.Our results show that PP1cB knockdown significantly reduces endothelial cell migration, but does not have any significant effect on endothelial tube formation. Endothelial cell migration in the knockdown group is restored to the control level of migration upon consecutive transfection with PP1cB cDNA. PP1cB overexpression does not significantly affect endothelial cell migration. The current study implies that PP1cB is a regulator of endothelial cell migration, which is critical in the process of angiogenesis. PP1cB may reduce endothelial cell migration through focal adhesion turnover and actin polymerization pathways. Further investigation regarding the role of PP1cB in the regulation of angiogenesis is required.