Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system

Ohno, Yusuke; Kashio, Atsushi; Ogata, Ren et al.

Molecular Biology of the Cell, 2012, 23(23), 4543-4551

Permalink : https://hdl.handle.net/2115/52126

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アクセス権
open access
URI
https://hdl.handle.net/2115/52126
タイトル
Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system
著者
Ohno, Yusuke ; Kashio, Atsushi ; Ogata, Ren ; Ishitomi, Akihiro ; Yamazaki, Yuki ; Kihara, Akio
著者名
Ohno, Yusuke
著者名
Kashio, Atsushi
著者名
Ogata, Ren
著者名
Ishitomi, Akihiro
著者名
Yamazaki, Yuki
e-Rad_Researcher
50333620
著者名
Kihara, Akio
言語
英語
発行日
2012-12-01
出版者
American Society for Cell Biology
収録物名
Molecular Biology of the Cell
巻(号)
23(23)
ページ
4543-4551
抄録
Palmitoylation plays important roles in the regulation of protein localization, stability, and activity. The protein acyltransferases (PATs) have a common DHHC Cys-rich domain. Twenty-three DHHC proteins have been identified in humans. However, it is unclear whether all of these DHHC proteins function as PATs. In addition, their substrate specificities remain largely unknown. Here we develop a useful method to examine substrate specificities of PATs using a yeast expression system with six distinct model substrates. We identify 17 human DHHC proteins as PATs. Moreover, we classify 11 human and 5 yeast DHHC proteins into three classes (I, II, and III), based on the cellular localization of their respective substrates (class I, soluble proteins; class II, integral membrane proteins; class III, lipidated proteins). Our results may provide an important clue for understanding the function of individual DHHC proteins.
資源タイプ
学術雑誌論文
出版タイプ
Version of Record
PISSN
1059-1524
関連情報 (isIdenticalTo)
出版社版DOI
https://doi.org/10.1091/mbc.E12-05-0336