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

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

Authors

  • Yaffe MB
  • Schutkowski M
  • Shen M
  • Zhou XZ
  • Stukenberg PT
  • Rahfeld JU
  • Xu J
  • Kuang J
  • Kirschner MW
  • Fischer G
  • Cantley LC
  • Lu KP

Journal

Science (New York, N.Y.)

Publication Data

December 12, 1997

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM56203
  • Agency: NIGMS NIH HHS, Id: GM56230
  • Agency: NIGMS NIH HHS, Id: R01 GM056203

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