Pleckstrin homology domain of phospholipase D2 is a negative regulator of focal adhesion kinase

Mi Kyoung Kim, Won Chan Hwang, Do Sik Min

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1 Citation (Scopus)


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.

Original languageEnglish
Pages (from-to)112-117
Number of pages6
JournalBMB reports
Issue number2
Publication statusPublished - 2021

Bibliographical note

Funding Information:
This work was supported by a National Research Foundation

Funding Information:
of Korea (NRF) grant funded by the Korean government (NRF-2018R1A2B3002179, 2019M3A9A8065095) and by the Yonsei University Research Fund (2019-22-0193).

Publisher Copyright:
© 2021. by the The Korean Society for Biochemistry and Molecular Biology.

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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