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KMID : 0624620210540020112
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BMB Reports
2021 Volume.54 No. 2 p.112 ~ p.117
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Pleckstrin homology domain of phospholipase D2 is a negative regulator of focal adhesion kinase
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Kim Mi-Kyoung
Hwang Won-Chan
Min Do-Sik
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Abstract
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Phospholipase D2 (PLD2) has been implicated in the tyrosine kinase-mediated signaling pathways, but the regulation events are yet to be identified. Herein, we demonstrate that pleckstrin homology (PH) domain of PLD2 (PLD2-PH) exerts an antitumorigenic effect via the suppression of PLD2 and focal adhesion kinase (FAK). The kinase domain of FAK interacts with PLD2-PH and induces tyrosine phosphorylation and activation of PLD2. Furthermore, PLD2 increased tyrosine phosphorylation of FAK. However, ectopic expression of the PLD2-PH competes for binding to FAK and reduces the interaction between PLD2 and FAK, thereby suppressing FAK-induced PLD activation and tyrosine phosphorylation of FAK. The PLD2-PH suppressed the migration and invasion of glioblastoma cells, as well as tumor formation in a xenograft mouse model. This study uncovers a novel role of PLD2-PH as a negative regulator of PLD2 and FAK.
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KEYWORD
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Focal adhesion kinase, Phospholipase D2, Pleckstrin homology domain, Tumorigenesis, Tyrosine phosphorylation
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