Proteomic and yeast 2-hybrid screens to identify PTEN binding partners

Priyanka Tibarewal, Laura Spinelli, Helene Maccario, Nicholas R. Leslie

Research output: Contribution to journalArticlepeer-review

2 Downloads (Pure)


PTEN is a phosphoinositide lipid phosphatase and an important tumour suppressor protein. PTEN function is reduced or lost in around a third of all human cancers through diverse mechanisms, from gene deletion to changes in the function of proteins which regulate PTEN through direct protein binding. Here we present data from SILAC (Stable Isotope Labelling by Amino acids in Cell culture) proteomic screens to identify proteins which bind to PTEN. These experiments using untransformed epithelial cells and glioma cells identified several novel candidate proteins in addition to many previously identified PTEN binding partners and many proteins which are recognised as common false positives using these methods. From subsequent co-expression pull-down experiments we provide further evidence supporting the physical interaction of PTEN with MMP1, Myosin 18A and SHROOM3. We also performed yeast two-hybrid screens which identify the previously recognised PTEN binding partner MSP58 in addition to the nuclear import export receptor TNPO3. These experiments identify several novel candidate binding partners of PTEN and provide further data addressing the set of proteins that interact with this important tumour suppressor.
Original languageEnglish
Article number100989
JournalAdvances in Biological Regulation
Early online date4 Oct 2023
Publication statusE-pub ahead of print - 4 Oct 2023


  • PDZ
  • Phosphatase
  • Protein-protein interaction
  • Proteomics
  • PTEN
  • Tumour suppressor

ASJC Scopus subject areas

  • Genetics
  • Molecular Medicine
  • Molecular Biology
  • Cancer Research


Dive into the research topics of 'Proteomic and yeast 2-hybrid screens to identify PTEN binding partners'. Together they form a unique fingerprint.

Cite this