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How ERK1/2 activation controls cell proliferation and cell death: Is subcellular localization the answer?
Yohannes Mebratu1, Yohannes Tesfaigzi
1Lovelace Respiratory Research Institute, 2425 Ridgecrest Drive SE, Albuquerque, NM 87108, USA.
Cell Cycle (Georgetown, Tex.)
|March 14, 2009
Summary
Extracellular signal-regulated protein kinases 1 and 2 (ERK1/2) can trigger cell death by remaining in the cytoplasm. This mechanism, distinct from their role in proliferation, offers new therapeutic targets for cancer and inflammatory diseases.
Area of Science:
- Molecular Biology
- Cell Signaling
- Apoptosis Research
Background:
- The Ras-Raf-MEK-ERK signaling pathway is crucial for cell proliferation but its role in cell death is less understood.
- Extracellular signal-regulated protein kinases 1 and 2 (ERK1/2) are key components of this pathway.
Purpose of the Study:
- To review recent findings on ERK1/2 translocation to the nucleus and mechanisms of cytosolic retention.
- To elucidate the role of cytosolic ERK1/2 in apoptosis and its potential as a therapeutic target.
Main Methods:
- Literature review of recent research papers.
- Focus on studies defining ERK1/2 nuclear translocation and cytosolic retention mechanisms.
- Analysis of proteins involved in regulating ERK1/2 localization and function.
Main Results:
- Cytosolic retention of ERK1/2 prevents interaction with nuclear transcription factors, inhibiting proliferative signals.
- Cytosolic ERK1/2 can enhance the activity of pro-apoptotic proteins, such as DAP kinase.
- This cytosolic function of ERK1/2 contributes to programmed cell death.
Conclusions:
- Understanding cytosolic ERK1/2 function is critical for elucidating cell death mechanisms.
- Targeting the cytosolic ERK1/2 pathway may offer novel therapeutic strategies for cancer and chronic inflammatory diseases.
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