A double point mutation in PCL-gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation
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- Title
- A double point mutation in PCL-gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation
- Authors
- Chung, SH; Kim, SK; Kim, JK; Yang, YR; Suh, PG; Chang, JS
- Date Issued
- 2010-03-31
- Publisher
- KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
- Abstract
- Growth factor stimulation induces Y783 phosphorylation of phosphoinositide-specific PLC-gamma 1, and the subsequent activation of this enzyme in a cellular signaling cascade. Previously, we showed that a double point mutation, Y509A/F510A, of PLC-gamma 1, abolished interactions with translational elongation factor 1-alpha. Here, we report that the Y509A/F510A mutant PLC-gamma 1 displayed extremely high levels of Y783 phosphorylation and enhanced catalytic activity, compared to wild-type PLC-gamma 1, upon treatment of COS7 cells with EGF. In quiescent COS7 cells, the Y509A/F510A mutant PLC-gamma 1 exhibited a constitutive hydrolytic activity, whereas the wild-type counterpart displayed a basal level of activity. Upon treatment of COS7 cells with EGF, the Y783F mutation in Y509A/F510A PLC-gamma 1 (Y509A/F510A/Y783F triple mutant) cells also led to an enhanced catalytic activity, whereas Y783F mutation alone displayed a basal level of activity. Our results collectively suggest that the Y509A/F510A mutant is more susceptible to receptor tyrosine kinase-induced Y783 phosphorylation than is wild-type PLC-gamma 1, but no longer requires Y783 phosphorylation step for the Y509A/F510A mutant PLC-gamma 1 activation in vivo.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/10203
- DOI
- 10.3858/EMM.2010.42.3.023
- ISSN
- 1226-3613
- Article Type
- Article
- Citation
- EXPERIMENTAL AND MOLECULAR MEDICINE, vol. 42, no. 3, page. 216 - 222, 2010-03-31
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