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Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system
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)
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Submitter: 木原 章雄
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