The effects of protein phosphorylation and dephosphorylation upon high-light-induced degradation of the photosystem II reaction center proteins D1 and D2 have been studied in isolated thylakoid membranes and photosystem II core complexes. The rate of photoinactivation of photosystem II electron transport is not affected by thylakoid membrane phosphorylation. However, the degradation rate of the D1-protein in its phosphorylated form is drastically reduced under conditions which induce either acceptor- or donor-side photoinhibition of photosystem II. The degradation rate of the D2-protein is also reduced following protein phosphorylation. The stability of the phosphorylated D1-protein is further increased under conditions of reduced phosphatase activity, suggesting that phosphorylated and damaged D1-protein has to be dephosphorylated prior to proteolytic degradation. Our results expand on experiments performed in vivo, which suggest that following photoinhibition the controlled repair of damaged photosystem II centers requires not only proteolytic enzymes but also kinase and phosphatase activities. It is suggested that the phosphorylation of the D1- and D2-proteins allows tight coordination of the degradation of damaged proteins with insertion of new copies of proteins into photosystem II.