Physical and functional interactions between hnRNP K and PRMT family proteins.
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.
Chan
James Yi-Hsin
JY
Graduate Institute of Medical Sciences, National Defense Medical Center, Room 7102, 161, Section 6, MinChuan, Taipei 114, Taiwan, ROC.
Hsieh
Tsai-Yuan
TY
Liu
Shu-Ting
ST
Chou
Wei-Yuan
WY
Chung
Min-Huey
MH
Huang
Shih-Ming
SM
D001120:Arginine / Q000378:metabolism; D006367:HeLa Cells; D034641:Heterogeneous-Nuclear Ribonucleoprotein K / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D025941:Protein Interaction Mapping; D011484:Protein-Arginine N-Methyltransferases / Q000235:genetics / Q000378:metabolism*; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D014758:Viral Core Proteins / Q000378:metabolism
D034641:Heterogeneous-Nuclear Ribonucleoprotein K; D012097:Repressor Proteins; D014758:Viral Core Proteins; C069130:nucleocapsid protein, Hepatitis C virus; D001120:Arginine; C099988:PRMT1 protein, human; D011484:Protein-Arginine N-Methyltransferases; C119966:coactivator-associated arginine methyltransferase 1