AbstractWe examined whether the phosphorylation of a 34 kDa lipocortin I-like protein may be associated with internalization process of fibroblast growth factor (FGF) in human umbilical vein endothelial (HUVE) cells. We show that: 1) exposure of synchronized HUVE cells to basic FGF for an appreciable time lag (≥30 min) at 37°C and subsequent phosphorylation at 37°C are required to obtain an increased32P-labelling of a 34 kDa substrate; 2) this FGF-stimulated phosphorylation occurs in S phase but not G1 phase of the growth cycle; 3) the 34 kDa substrate appears to be phosphorylated on tyrosine residues; 4) a major fraction of the 34 kDa32P-labelled substrate is immunoprecipitated with an antibody that has been raised against human lipocortin/annexin of type I. It is suggested that internalized FGF-receptor/kinase complexes might be primarily responsible for the phosphorylation of the 34 kDa lipocortin I-related protein in S phase HUVE cells.