ATP-induced focal adhesion kinase activity is negatively modulated by phospholipase D2 in PC12 cells
SCIE
SCOPUS
KCI
- Title
- ATP-induced focal adhesion kinase activity is negatively modulated by phospholipase D2 in PC12 cells
- Authors
- Bae, YS; Ryu, SH
- Date Issued
- 2001-09-30
- Publisher
- KOREAN SOC MED BIOCHEMISTRY MOLECULAR
- Abstract
- Extracellular ATP has been known to modulate various cellular responses including mitogenesis, secretion and morphogenic activity in neuronal cells. In the ATP-incluced morphogenic activity, focal adhesion kinase(s) such as Fak have been suggested to play a critical role. Binding of ATP to its specific cell surface receptor in PC12 cells induces phospholipase D (PLO) activity. However, the role of PLD on ATP-induced Fak activation in PC12 cells remains unclear. In this study, we investigated the role of PLD on the ATP-induced Fak activation and paxillin phosphorylation using two established cell lines: wild type PLD2- and lipase-inactive mutant PLD2-inducible PC12 cells. Stimulation of cells with ATP caused PLD2 activation via classical protein kinase C activation. ATP also induced Fak activation, and paxillin phosphorylation, and were dramatically reduced by wild type PLD2 overexpression but not by lipase-inactive mutant PLD2 overexpression. When the PC12 cells were pretreated with propranolol, a specific inhibitor for phosphatidic acid phosphohydrolase resulting in the accumulation of PA, ATP-induced Fak-activation and paxillin phosphorylation were also reduced. We found that inhibition of tyrosine phosphatases by pervanadate completely blocked PLD2-dependent Fak and paxillin dephosphorylation. Taken together, we suggest that PLD2 activity might play a negative role in ATP-induced Fak and paxillin phosphorylation possibly through tyrosine phosphatases.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/10185
- DOI
- 10.1038/emm.2001.26
- ISSN
- 1226-3613
- Article Type
- Article
- Citation
- EXPERIMENTAL AND MOLECULAR MEDICINE, vol. 33, no. 3, page. 150 - 155, 2001-09-30
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