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Investigating Methylated Arginine Residues in PGC‐1α
Author(s) -
Cuala Janielle Miguel,
Osuji Immaculeta Miguel,
ZuritaLopez Cecilia
Publication year - 2017
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.31.1_supplement.lb141
Subject(s) - arginine , methylation , context (archaeology) , coactivator , biochemistry , phosphorylation , biology , chemistry , amino acid , gene , transcription factor , paleontology
Peroxisome proliferator‐activated receptor γ coactivator 1α (PGC‐1α) participates in the regulation of both carbohydrate and lipid metabolism and is activated by insulin. For these reasons, it has been implicated in obesity and diabetes. PGC‐1α is subjected to many post‐translational modifications including phosphorylation of Ser570 by protein kinase B (Akt/PKB), which stops gluconeogenesis and fatty acid oxidation. In addition, PGC‐1α is methylated by protein arginine methyltransferase 1 (PRMT1) at several arginine residues, including Arg665, Arg667 and Arg669 which enhance its regulation. Evidence for additional arginine methylated sites have been found, but the exact sites remain unknown. We set out to identify methylated arginine residues on PGC‐1α. PRMT1 and truncated constructs corresponding to PGC‐1α were expressed and purified. Next, in vitro methylation reactions were carried out, followed by detection of methylated arginine residues by various methods including immunoblot and autoradiography. Identification of the methylated arginine residue(s), will enhance our understanding of PGC‐1α with the broader goal of determining its regulation in the context of obesity and diabetes. Support or Funding Information Minority Biomedical Research Support‐Research Initiative for Scientific Enhancement (MBRS‐RISE) Fellowship. Grant: R25 GM061331