Active Pin1 is a key target of all-trans retinoic acid in acute promyelocytic leukemia and breast cancer

Nat Med. 2015 May;21(5):457-66. doi: 10.1038/nm.3839. Epub 2015 Apr 13.

Abstract

A common key regulator of oncogenic signaling pathways in multiple tumor types is the unique isomerase Pin1. However, available Pin1 inhibitors lack the required specificity and potency for inhibiting Pin1 function in vivo. By using mechanism-based screening, here we find that all-trans retinoic acid (ATRA)--a therapy for acute promyelocytic leukemia (APL) that is considered the first example of targeted therapy in cancer, but whose drug target remains elusive--inhibits and degrades active Pin1 selectively in cancer cells by directly binding to the substrate phosphate- and proline-binding pockets in the Pin1 active site. ATRA-induced Pin1 ablation degrades the protein encoded by the fusion oncogene PML-RARA and treats APL in APL cell and animal models as well as in human patients. ATRA-induced Pin1 ablation also potently inhibits triple-negative breast cancer cell growth in human cells and in animal models by acting on many Pin1 substrate oncogenes and tumor suppressors. Thus, ATRA simultaneously blocks multiple Pin1-regulated cancer-driving pathways, an attractive property for treating aggressive and drug-resistant tumors.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Agents / chemistry
  • Breast Neoplasms / genetics
  • Breast Neoplasms / metabolism*
  • Catalysis
  • Catalytic Domain
  • Cell Line, Tumor
  • Dose-Response Relationship, Drug
  • Female
  • Fibroblasts / metabolism
  • Gene Expression Regulation, Leukemic*
  • Gene Expression Regulation, Neoplastic*
  • HEK293 Cells
  • Humans
  • Leukemia, Promyelocytic, Acute / genetics
  • Leukemia, Promyelocytic, Acute / metabolism*
  • MCF-7 Cells
  • Mice
  • Mice, Inbred BALB C
  • Mice, Knockout
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Neoplasm Transplantation
  • Peptidylprolyl Isomerase / genetics*
  • Phosphates / chemistry
  • Phosphorylation
  • Proline / chemistry
  • Tretinoin / metabolism*
  • Triple Negative Breast Neoplasms / metabolism

Substances

  • Antineoplastic Agents
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Phosphates
  • Tretinoin
  • Proline
  • PIN1 protein, human
  • Peptidylprolyl Isomerase
  • Pin1 protein, mouse

Associated data

  • GEO/GSE63059
  • PDB/4TNS