Hacking RNA: Hakai promotes tumorigenesis by enhancing the RNA-binding function of PSF

Cell Cycle. 2009 Nov 15;8(22):3648-51. doi: 10.4161/cc.8.22.9909. Epub 2009 Nov 24.

Abstract

Hakai, an E3 ubiquitin ligase for the E-cadherin complex, plays a crucial role in lowering cell-cell contacts in epithelial cells, a hallmark feature of tumor progression. Recently, Hakai was also found to interact with PSF (PTB-associated splicing factor). While PSF can function as a DNA-binding protein with a tumor suppressive function, its association with Hakai promotes PSF's RNA-binding ability and post-transcriptional influence on target mRNAs. Hakai overexpression enhanced the binding of PSF to mRNAs encoding cancer-related proteins, while knockdown of Hakai reduced the RNA-binding ability of PSF. Furthermore, the knockdown of PSF suppressed Hakai-induced cell proliferation. Thus, Hakai can affect the oncogenic phenotype both by altering E-cadherin-based intercellular adhesions and by increasing PSF's ability to bind RNAs that promote cancer-related gene expression.

Publication types

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

MeSH terms

  • Cadherins / metabolism*
  • Cell Proliferation*
  • Humans
  • Models, Biological
  • Neoplasms / genetics*
  • Oncogene Proteins / metabolism
  • Oncogene Proteins / physiology*
  • PTB-Associated Splicing Factor
  • Protein Binding
  • RNA, Messenger / metabolism
  • RNA, Messenger / physiology*
  • RNA-Binding Proteins / metabolism*
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitin-Protein Ligases / physiology*

Substances

  • Cadherins
  • Oncogene Proteins
  • PTB-Associated Splicing Factor
  • RNA, Messenger
  • RNA-Binding Proteins
  • CBLL1 protein, human
  • Ubiquitin-Protein Ligases