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. Structured summary: MINT-6803853:. hnRPK, (uniprotkb:P61978) binds (MI:0407) to PRMT1 (uniprotkb:Q99873) by pull down (MI:0096). MINT-6803884:. hnRPK, (uniprotkb:P61978) physically interacts (MI:0218) with CARM1 (uniprotkb:Q86X55) by anti tag coimmunoprecipitation (MI:0007). MINT-6803869:. hnRPK, (uniprotkb:P61978) physically interacts (MI:0218) with PRMT1 (uniprotkb:Q99873) by anti tag coimmunoprecipitation (MI:0007). MINT-6803939:. hnRPK, (uniprotkb:P61978) binds (MI:0407) to PRMT2 (uniprotkb:P55345) by pull down (MI:0096). MINT-6803929:. hnRPK, (uniprotkb:P61978) binds (MI:0407) to RMT (uniprotkb:P38074) by pull down (MI:0096). MINT-6803896:. hnRPK, (uniprotkb:P61978) binds (MI:0407) to PRMT3 (uniprotkb:O60678) by pull down (MI:0096). MINT-6803834:. PRMT1 (uniprotkb:Q99873) methylates (MI:0213) hnRPK, (uniprotkb:P61978) by methyltransferase assay (MI:0515).
Original language | English |
---|---|
Pages (from-to) | 281-286 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 583 |
Issue number | 2 |
DOIs | |
Publication status | Published - Jan 22 2009 |
Keywords
- HCV Core protein
- hnRNP K
- PRMT
- Protein-protein interaction
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology