Cullin 3 targets methionine adenosyltransferase IIα for ubiquitylation-mediated degradation and regulates colorectal cancer cell proliferation

FEBS J. 2016 Jul;283(13):2390-402. doi: 10.1111/febs.13759. Epub 2016 Jun 6.

Abstract

Cullin 3 (CUL3) serves as a scaffold protein and assembles a large number of ubiquitin ligase complexes. It is involved in multiple cellular processes and plays a potential role in tumor development and progression. In this study, we demonstrate that CUL3 targets methionine adenosyltransferase IIα (MAT IIα) and promotes its proteasomal degradation through the ubiquitylation-mediated pathway. MAT IIα is a key enzyme in methionine metabolism and is associated with uncontrolled cell proliferation in cancer. We presently found that CUL3 down-regulation could rescue folate deprivation-induced MAT IIα exhaustion and growth arrest in colorectal cancer (CRC) cells. Further results from human CRC samples display an inverse correlation between CUL3 and MAT IIα protein levels. Our observations reveal a novel role of CUL3 in regulating cell proliferation by controlling the stability of MAT IIα.

Keywords: MAT IIα; colorectal cancer; cullin 3; folate; ubiquitin.

Publication types

  • Editorial
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Cell Proliferation / drug effects
  • Cell Proliferation / genetics
  • Colorectal Neoplasms / enzymology*
  • Colorectal Neoplasms / genetics
  • Colorectal Neoplasms / physiopathology
  • Cullin Proteins / genetics
  • Cullin Proteins / metabolism*
  • Folic Acid / genetics
  • Folic Acid / metabolism
  • HCT116 Cells
  • HEK293 Cells
  • Histone Deacetylase Inhibitors / pharmacology
  • Humans
  • Immunoprecipitation
  • In Vitro Techniques
  • Methionine Adenosyltransferase / chemistry
  • Methionine Adenosyltransferase / genetics
  • Methionine Adenosyltransferase / metabolism*
  • Proteolysis
  • RNA Interference
  • Ubiquitination / drug effects
  • Ubiquitination / genetics

Substances

  • CUL3 protein, human
  • Cullin Proteins
  • Histone Deacetylase Inhibitors
  • Folic Acid
  • Methionine Adenosyltransferase