Phosphatidylinositol 3-kinase/Akt activity regulates c-FLIP expression in tumor cells

D J Panka1, T Mano, T Suhara

  • 1Department of Hematology and Oncology, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215, USA.

Insights

The phosphatidylinositol 3-kinase (PI3K)-Akt pathway, not MEK1, regulates FLICE-inhibitory protein (FLIP) in tumor cells. This pathway controls FLIP expression, impacting apoptosis resistance and offering potential therapeutic targets.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Signaling

Background:

  • FLICE-inhibitory protein (FLIP) inhibits apoptosis by blocking caspase-8 activation.
  • FLIP expression is linked to resistance against tumor necrosis factor (TNF) family-induced apoptosis and Fas-mediated cell death.
  • While MEK1 regulates FLIP in T cells, the pathways controlling FLIP in tumor cells remain unclear.

Purpose of the Study:

  • To investigate the roles of MAP kinase and phosphatidylinositol 3-kinase (PI3K) signaling pathways in regulating FLIP expression in tumor cells.

Main Methods:

  • Treatment of tumor cell lines with MEK1 inhibitor PD98059 and PI3K inhibitor LY294002.
  • Assessment of FLIP protein and mRNA levels, and Akt phosphorylation.
  • Utilized dominant-negative and constitutively active Akt adenoviral constructs to modulate Akt activity.

Main Results:

  • MEK1 inhibition only affected FLIP levels in a minority of tumor cell lines.
  • PI3K pathway disruption with LY294002 consistently reduced FLIP protein/mRNA and Akt phosphorylation across all tested cell lines.
  • Modulation of Akt activity via adenoviral constructs directly altered FLIP expression and Akt target phosphorylation (GSK-3).

Conclusions:

  • The PI3K-Akt pathway, rather than MEK1, is a key regulator of FLIP expression in tumor cells.
  • These findings identify FLIP as another apoptosis inhibitor regulated by the PI3K-Akt pathway, suggesting potential therapeutic implications.

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
Interactions Between Signaling Pathways01:19

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a rapamycin-insensitive companion...