Palmitoylation in Regulating Fyn Kinase Activity Based on FRET Imaging
10.16156/j.1004-7220.2023.02.04
- VernacularTitle:基于 FRET 成像探究棕榈酰化修饰调节 Fyn 激酶活性
- Author:
Xin ZHANG
1
,
2
;
Jia GUO
3
;
Hui YAO
1
,
2
;
Linhong DENG
3
;
Mingxin OUYANG
3
Author Information
1. Institute of Biomedical Engineering and Health Sciences, School of Medical and Health Engineering
2. School of Pharmacy & School of Biological and Food Engineering, Changzhou University
3. Institute of Biomedical Engineering and Health Sciences, School of Medical and Health Engineering, Changzhou University
- Publication Type:Journal Article
- Keywords:
Fyn kinase;
palmitoylation;
fluorescence resonance energy transfer (FRET);
CSK kinase
- From:
Journal of Medical Biomechanics
2023;38(2):E228-E235
- CountryChina
- Language:Chinese
-
Abstract:
Objective To investigate the molecular mechanism of palmitoylation modification in regulating the activity of non-receptor tyrosine kinase Fyn. Methods The intracellular Fyn activity was detected by applying fluorescence resonance energy transfer (FRET) technology, and the mechanism was investigated by combining with Fyn palmitoylation deficiency and C-terminal Src kinase ( CSK ) plasmid co-expression. ResultsExperimental data showed that single loss of either of ( C3, C6) palmitoylation sites resulted in higher Fyn activity, and C6 seemed more significant. It is known that CSK membrane translocation occurred after activation. FRET assay confirmed that CSK could down-regulate the activity of Fyn in cells, but could not effectively regulate the activity of Fyn(GSS) with the loss of palmitoylation sites. Conclusions The results in this study support the hypothesis on Fyn regulation by spatial localization, namely, non-palmitoylated Fyn (GSS) is less effective in the inhibitory regulation by CSK on cell membrane, thus promoting constitutive high activity expression
