Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 23, Issue 23, Pages 4543-4551Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E12-05-0336
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Funding
- Japan Society for the Promotion of Science [23370057]
- Grants-in-Aid for Scientific Research [23370057] Funding Source: KAKEN
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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.
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