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Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism.

Science (New York, N.Y.) | Dec 12, 1997

http://www.ncbi.nlm.nih.gov/pubmed/9395400

Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). In response to their phosphorylation during mitosis, Pin1 binds and regulates members of a highly conserved set of proteins that overlaps with antigens recognized by the mitosis-specific monoclonal antibody MPM-2. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization.

Pubmed ID: 9395400 RIS Download

Mesh terms: Amino Acid Isomerases | Antibodies, Monoclonal | Binding Sites | Carrier Proteins | Cell Cycle Proteins | DNA-Binding Proteins | Epitopes | HeLa Cells | Heat-Shock Proteins | Humans | Isomerism | Mitosis | Models, Molecular | Oligopeptides | Peptide Library | Peptidylprolyl Isomerase | Phosphoproteins | Phosphorylation | Phosphoserine | Phosphothreonine | Proline | Protein Conformation | Recombinant Fusion Proteins | Substrate Specificity | Tacrolimus Binding Proteins