Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

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

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

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 | NIMA-Interacting Peptidylprolyl Isomerase | Oligopeptides | Peptide Library | Peptidylprolyl Isomerase | Phosphoproteins | Phosphorylation | Phosphoserine | Phosphothreonine | Proline | Protein Conformation | Recombinant Fusion Proteins | Substrate Specificity | Tacrolimus Binding Proteins