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Physical and functional interactions between hnRNP K and PRMT family proteins
Author(s) -
Huang ShihMing,
Hsieh TsaiYuan,
Liu ShuTing
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.713.3
Subject(s) - coactivator , transactivation , immunoprecipitation , methylation , biology , genetics , microbiology and biotechnology , gene , gene expression , transcription factor
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. In summary, the indirect binding ability of PRMT proteins and the arginine methylation status of hnRNP K protein are not necessary for the coactivator functions of these working complexes, suggesting that other factors determine their functional roles in some transcriptional systems. (Research support from National Science Council, Taipei, Taiwan, Republic of China, to Shih‐Ming Huang)