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From receptors to stress-activated MAP kinases
1Department of Biomaterials Science, Faculty of Dentistry, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan.
Oncogene
|November 11, 1999
Summary
Stress-activated protein kinases, including JNK and p38 MAP kinases, regulate cell fate. This review explores how inflammatory signals reach these key stress-activated MAP kinase cascades.
Area of Science:
- Cellular Biology
- Molecular Biology
- Signal Transduction
Background:
- Cell fate decisions (life, death, differentiation) are governed by intracellular signals.
- Stress-activated protein kinases, such as JNK and p38 MAP kinases, play a crucial role in these decisions.
- The precise mechanisms linking external stimuli to these kinases remain unclear.
Purpose of the Study:
- To review the molecular links between inflammatory cytokine receptors and stress-activated MAP kinase pathways.
- To elucidate the upstream signaling events in JNK and p38 activation.
- To provide an overview of current knowledge on stress-activated MAP kinase signaling.
Main Methods:
- Literature review of stress-activated MAP kinase pathways.
- Analysis of molecular mechanisms in cell signaling.
- Focus on inflammatory cytokine receptor signaling.
Main Results:
- JNK and p38 MAP kinases are central to stress-induced cell fate determination.
- Extracellular signals are transmitted via complex cascades from receptors to kinases.
- Understanding these pathways is crucial for deciphering cell survival and death.
Conclusions:
- The molecular mechanisms connecting inflammatory cytokine receptors to JNK and p38 MAP kinase cascades are under active investigation.
- Further research is needed to fully understand these critical cell signaling pathways.
- This review consolidates current knowledge on these essential cellular processes.