Physical and functional interactions between hnRNP K and PRMT family proteins

FEBS Lett. 2009 Jan 22;583(2):281-6. doi: 10.1016/j.febslet.2008.12.025. Epub 2008 Dec 26.

Abstract

The mechanism underlying the protein-protein interaction of hnRNP K and PRMT family proteins is unclear. We examined and confirmed the arginine methylation of hnRNP K protein by PRMT1, not CARM1, via their direct binding. We also studied hnRNP K protein complexes containing CARM1, as well as PRMT1, using co-immunoprecipitation analysis. PRMT family proteins might be involved in the regulation of hnRNP K functions in nuclear receptor coactivator, transactivation, and p21 gene and protein expressions. We believe these observations will help provide insights into the regulation of hnRNP K protein functions via the recruitment of its associated proteins, including its arginine methylation-modifying proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arginine / metabolism
  • HeLa Cells
  • Heterogeneous-Nuclear Ribonucleoprotein K / genetics
  • Heterogeneous-Nuclear Ribonucleoprotein K / metabolism*
  • Humans
  • Methylation
  • Protein Interaction Mapping
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Viral Core Proteins / metabolism

Substances

  • Heterogeneous-Nuclear Ribonucleoprotein K
  • Repressor Proteins
  • Viral Core Proteins
  • nucleocapsid protein, Hepatitis C virus
  • Arginine
  • PRMT1 protein, human
  • Protein-Arginine N-Methyltransferases
  • coactivator-associated arginine methyltransferase 1