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The peptidyl prolyl  cis / trans  isomerase (PPIase) Pin1 plays an important role in phosphorylation-dependent events of the cell cycle. This function is linked to its display of two phosphothreonine/phosphoserine-proline binding motifs, one within the type IV WW domain and a second within the parvulin-like catalytic domain. By microinjection of the compound Ac-Phe-D-Thr(PO 3 H 2 )-Pip-Nal-Gln-NH 2 , which inhibits  Xenopus laevis  Pin1 with a  K  i  value of 19.4±1.5 nM, into the animal pole of  X. laevis  embryos at the two-cell stage, the impact of Pin1 PPIase activity on cell cycle progression and embryonic development could be analysed, independent of WW domain-mediated phosphoprotein binding. Injected embryos showed a dramatically decreased survival rate at late stages of development that could only be partially compensated by co-injection with mRNAs of enzymatically active Pin1 variants, demonstrating that the phosphorylation-specific PPIase activity of Pin1 is essential for cell division and development in  X. laevis .

An essential role for Pin1 in Xenopus laevis embryonic development revealed by specific inhibitors