Identification of posttranslational modifications in peroxisome proliferator-activated receptor γ using mass spectrometry

Shogo Katsura, Tomoko Okumura, Ryo Ito, Akira Sugawara, Atsushi Yokoyama

研究成果: Article査読

7 被引用数 (Scopus)

抄録

Posttranslational modification (PTM) of proteins is critical for various cellular processes. However, there are few studies examining PTMs in specific proteins using unbiased approaches. Here we report the attempt to identify the PTMs in peroxisome proliferator-activated receptor γ (PPARγ) proteins using our previously established PTM analysis system. In this study, we identified several PTMs in exogenously expressed PPARγ2 proteins from 293T cells as well as endogenous PPARγ1 proteins from a Caco-2 colon cancer cell line. The identified PTMs include phosphorylation of serine 112 and serine 81 in PPARγ2 and PPARγ1, respectively, both of which are well-known mitogen-activated protein kinase- (MAP kinase-) mediated PTMs in PPARγ proteins, thus confirming our experimental approach. Furthermore, previously unknown PTMs were also identified, demonstrating that this method can be applied to find previously unidentified PTMs in PPARγ proteins and other proteins including nuclear receptors.

本文言語English
論文番号468925
ジャーナルPPAR Research
2014
DOI
出版ステータスPublished - 2014

ASJC Scopus subject areas

  • 創薬
  • 薬理学(医学)

フィンガープリント

「Identification of posttranslational modifications in peroxisome proliferator-activated receptor γ using mass spectrometry」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル