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

BMB Reports 2021년 54권 2호 p.112 ~ 117
김미경, Hwang Won-Chan, 민도식,
소속 상세정보
김미경 ( Kim Mi-Kyoung ) - Pusan National University College of Natural Sciences Department of Molecular Biology
 ( Hwang Won-Chan ) - Pusan National University College of Natural Sciences Department of Molecular Biology
민도식 ( Min Do-Sik ) - Yonsei University College of Pharmacy

Abstract


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.

키워드

Focal adhesion kinase; Phospholipase D2; Pleckstrin homology domain; Tumorigenesis; Tyrosine phosphorylation

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