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Updated: May 22, 2026

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration
Published on: May 19, 2016
PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα12
Xiaoqing Gan1, Jiyong Wang, Chen Wang
1Department of Pharmacology and Program in Vascular Biology and Therapeutics, Yale School of Medicine, New Haven, Connecticut 06520, USA.
Abstract:
Mammalian target of rapamycin complex 2 (mTORC2) phosphorylates AGC protein kinases including protein kinase C (PKC) and regulates cellular functions such as cell migration. However, its regulation remains poorly understood. Here we show that lysophosphatidic acid (LPA) induces two phases of PKC-δ hydrophobic motif phosphorylation. The late phase is mediated by Gα(12), which specifically activates ARAF, leading to upregulation of the RFFL E3 ubiquitin ligase and subsequent ubiquitylation and degradation of the PRR5L subunit of mTORC2. Destabilization of PRR5L, a suppressor of mTORC2-mediated hydrophobic motif phosphorylation of PKC-δ, but not AKT, results in PKC-δ hydrophobic motif phosphorylation and activation. This Gα(12)-mediated signalling pathway for mTORC2 regulation is critically important for fibroblast migration and pulmonary fibrosis development.
Insights
Lysophosphatidic acid (LPA) triggers a novel signaling pathway involving Gα(12) and RFFL E3 ubiquitin ligase to regulate mTORC2 activity, impacting cell migration and pulmonary fibrosis.
Area of Science:
- Cellular Biology
- Molecular Signaling
- Biochemistry
Background:
- Mammalian target of rapamycin complex 2 (mTORC2) is crucial for cell migration by phosphorylating AGC kinases like protein kinase C (PKC).
- The precise regulatory mechanisms governing mTORC2 activity, particularly its hydrophobic motif phosphorylation, remain largely unelucidated.
- Understanding mTORC2 regulation is vital for addressing cellular dysfunction in diseases such as fibrosis.
Purpose of the Study:
- To elucidate the signaling pathway by which lysophosphatidic acid (LPA) regulates mTORC2.
- To investigate the role of specific signaling components, including Gα(12), ARAF, and RFFL, in mTORC2-mediated PKC-δ phosphorylation.
- To determine the functional significance of this pathway in fibroblast migration and the development of pulmonary fibrosis.
Main Methods:
- Investigated the two-phase phosphorylation of PKC-δ hydrophobic motif induced by LPA.
- Utilized Gα(12) signaling to identify downstream effectors, including ARAF activation and RFFL E3 ubiquitin ligase.
- Examined the ubiquitylation and degradation of the mTORC2 PRR5L subunit and its impact on PKC-δ and AKT phosphorylation.
- Assessed the role of the identified pathway in fibroblast migration and pulmonary fibrosis models.
Main Results:
- LPA induces a late-phase PKC-δ hydrophobic motif phosphorylation dependent on Gα(12).
- Gα(12) activates ARAF, leading to increased RFFL E3 ubiquitin ligase expression.
- RFFL mediates ubiquitylation and degradation of PRR5L, a suppressor of mTORC2 activity.
- PRR5L destabilization specifically enhances PKC-δ, not AKT, hydrophobic motif phosphorylation and activation.
- This pathway is essential for fibroblast migration and the pathogenesis of pulmonary fibrosis.
Conclusions:
- A novel Gα(12)-ARAF-RFFL signaling axis regulates mTORC2 by degrading PRR5L.
- This pathway specifically controls PKC-δ activation, influencing cell migration.
- The elucidated mechanism is critical for fibroblast migration and the development of pulmonary fibrosis, offering potential therapeutic targets.
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