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

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/52126

Title: Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system
Authors: Ohno, Yusuke Browse this author
Kashio, Atsushi Browse this author
Ogata, Ren Browse this author
Ishitomi, Akihiro Browse this author
Yamazaki, Yuki Browse this author
Kihara, Akio Browse this author →KAKEN DB
Issue Date: 1-Dec-2012
Publisher: American Society for Cell Biology
Journal Title: Molecular Biology of the Cell
Volume: 23
Issue: 23
Start Page: 4543
End Page: 4551
Publisher DOI: 10.1091/mbc.E12-05-0336
Abstract: 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.
Type: article
URI: http://hdl.handle.net/2115/52126
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 木原 章雄

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