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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Protein Kinase C delta-Mediated Phosphorylation of Phospholipase D Controls Integrin-Mediated Cell Spreading

Cited 13 times inthomson ciCited 10 times inthomson ci
Title
Protein Kinase C delta-Mediated Phosphorylation of Phospholipase D Controls Integrin-Mediated Cell Spreading
Author
Chae, Young ChanKim, Kyung LockHa, Sang HoonKim, JaeyoonSuh, Pann-GhillRyu, Sung Ho
Issue Date
2010-11
Publisher
AMER SOC MICROBIOLOGY
Citation
MOLECULAR AND CELLULAR BIOLOGY, v.30, no.21, pp.5086 - 5098
Abstract
Integrin signaling plays critical roles in cell adhesion, spreading, and migration, and it is generally accepted that to regulate these integrin functions accurately, localized actin remodeling is required. However, the molecular mechanisms that control the targeting of actin regulation molecules to the proper sites are unknown. We previously demonstrated that integrin-mediated cell spreading and migration on fibronectin are dependent on the localized activation of phospholipase D (PLD). However, the mechanism underlying PLD activation by integrin is largely unknown. Here we demonstrate that protein kinase Cδ (PKCδ) is required for integrin-mediated PLD signaling. After integrin stimulation, PKCδ is activated and translocated to the edges of lamellipodia, where it colocalizes with PLD2. The abrogation of PKCδ activity inhibited integrin-induced PLD activation and cell spreading. Finally, we show that Thr566 of PLD2 is directly phosphorylated by PKCδ and that PLD2 mutation in this region prevents PLD2 activation, PLD2 translocation to the edge of lamellipodia, Rac translocation, and cell spreading after integrin activation. Together, these results suggest that PKCδ is a primary regulator of integrin-mediated PLD activation via the direct phosphorylation of PLD, which is essential for directing integrin-induced cell spreading.
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DOI
10.1128/MCB.00443-10
ISSN
0270-7306
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BME_Journal Papers
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