Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients

Biochem Biophys Res Commun. 2006 Mar 24;341(4):1059-65. doi: 10.1016/j.bbrc.2005.12.228. Epub 2006 Jan 25.


The peptidyl-prolyl isomerase Pin1 is prevalently overexpressed in human cancers and is regarded as a new diagnostic and therapeutic target. Pin1 interacts with several proteins involved in cell cycle events in a phosphorylation-dependent manner. Among them, NIMA (never in mitosis, gene A) was first identified to interact with Pin1. In this report, we found that Pin1 could interact with Nek6, one of the human NIMA-related kinases (Neks). This interaction was confirmed by GST pull-down assay, which was further confirmed by immunoprecipitation experiments, as well as immunofluorescence colocalization. We further studied Pin1 and Nek6 mRNA level in 40 pairs of hepatocellular carcinoma cases, finding significant correlations between Nek6 and Pin1 mRNA expression levels in these samples.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Aged
  • Aged, 80 and over
  • Carcinoma, Hepatocellular / metabolism*
  • Carcinoma, Hepatocellular / ultrastructure
  • Cell Nucleus / metabolism
  • Female
  • Gene Expression Regulation, Neoplastic
  • Glutathione Transferase / chemistry
  • Humans
  • Immunoprecipitation / methods
  • Liver Neoplasms / metabolism*
  • Liver Neoplasms / ultrastructure
  • Male
  • Middle Aged
  • NIMA-Interacting Peptidylprolyl Isomerase
  • NIMA-Related Kinases
  • Peptidylprolyl Isomerase / chemistry
  • Peptidylprolyl Isomerase / metabolism*
  • Protein-Serine-Threonine Kinases / chemistry
  • Protein-Serine-Threonine Kinases / metabolism*


  • NIMA-Interacting Peptidylprolyl Isomerase
  • Glutathione Transferase
  • NEK6 protein, human
  • NIMA-Related Kinases
  • Protein-Serine-Threonine Kinases
  • PIN1 protein, human
  • Peptidylprolyl Isomerase