MAPK Signaling Pathways in Apoptosis Notes
MAPK Signaling Pathways in Apoptosis
Introduction
- MAPK (mitogen-activated protein kinase) signaling pathways regulate biological processes.
- MAPKs can activate or inhibit apoptosis depending on cell context.
- Discusses pro- and anti-apoptotic mechanisms regulated by MAPKs, signaling properties, and positive feedback loops.
- MAPKs’ behavior can be predicted based on stimulus intensity and duration.
- Highlights the multiple positive feedback loops in apoptosis.
MAPK Cascades
- MAPK family is activated by dual phosphorylation on a tripeptide motif (Thr-X-Tyr).
- Activation occurs through a three-tiered cascade: MAPK, MAPKK, and MAPKKK.
- MAPK inactivation is mediated by phosphatases via dephosphorylation.
- Scaffold proteins monitor activation and inactivation.
- Mammals have 14 MAPK members in 7 subgroups; 4 conventional and 3 atypical.
- MAPKs convert extracellular stimuli into cellular responses like growth, migration, proliferation, differentiation, and apoptosis.
JNK and p38 MAPK Cascades in Pro-Apoptotic Processes
- JNKs and p38 MAPKs balance cell survival and death from stresses.
- These kinases integrate signals, converging on caspase activation in a cell-specific manner.
- Caspases are activated by extrinsic or intrinsic pathways.
- Cytochrome c release is critical in the intrinsic pathway and is mediated by pro-apoptotic Bcl-2 proteins.
- Several Bcl-2 family proteins are under JNK and/or p38 MAPK control at transcriptional/post-transcriptional levels.
- Different JNK and p38 genes exist in vertebrates, but focus is on JNK1-1 and JNK1-2 in osmostress-induced apoptosis.
Transcriptional Regulation
- JNK and p38 MAPK substrates promote apoptosis.
- Transcription factors are regulated, increasing pro-apoptotic and decreasing anti-apoptotic protein expression.
- A major JNK target is AP-1, regulating cell proliferation, differentiation, survival, and apoptosis context-dependently.
- p53 tumor suppressor is regulated by JNK and p38 MAPK cascades in apoptosis.
- JNK-mediated phosphorylation stabilizes and activates p53, promoting programmed cell death.
- p53-p73 dimerization induces apoptotic cell death, particularly in response to JNK-mediated stress.
Post-Transcriptional Modifications
- JNK/p38 MAPK cascades regulate apoptotic proteins directly in both pathways.
- The extrinsic pathway induces caspase-8 activation, and in some cells, caspase-8 cleaves Bid, inducing cytochrome c release.
- The extrinsic and intrinsic pathways converge in the mitochondria.
- JNK phosphorylates iTCH, promoting degradation of c-FLIP.
- p38 and JNK regulate autophagy programs, with RIPK and JNK activation inducing autophagic cell death.
- JNK-mediated phosphorylation of 14-3-3 protein induces Bax release.
- JNK and p38 directly phosphorylate and regulate Bcl-2 family members, such as Bad, Bax, Bim, and Bmf.
JNK and p38 MAPK Cascades in Anti-Apoptotic Processes
Transcriptional Regulation examples:
- BNIP3 upregulation protects keratinocytes from UVB-induced apoptosis via ERK and JNK pathways.
- JNK activation attenuates ER-induced cell death by enhancing anti-apoptotic protein expression.
- TRPV6 expression via JNK protects hESC-CMs from apoptotic cell death.
- JNK/c-Jun signaling promotes annexin A2 overexpression, suppressing p53 expression.
- p38 MAPK induces Nur77 expression, enhancing cell survival via apoptosis suppression.
Post-Translational Regulation examples:
- Phosphorylation of caspase-9 at Thr125 by ERK1/2 restrains intrinsic apoptosis, with p38 MAPK catalyzing the phosphorylation during hyperosmotic stress.
- Transient JNK activation delays caspase-9 activation by direct interaction with Apaf 1 and cytochrome c.
- p38 MAPK/MK2 interacts with RIPK1, inhibiting RIPK1 auto-phosphorylation.
MAPK Signal Cross-Talks
- Crosstalk between JNK and p38 MAPK regulates stress responses.
- Pathways share upstream regulators, but p38 MAPK can negatively regulate JNK activity.
- Balance between JNK and p38 signaling determines cell fate.
- UV-C-induced p38 activation increases DUSP1 levels, protecting cells from UV-C-induced apoptosis by inactivating JNK.
The Two Faces of ERK in Apoptosis
- ERK1/2 activation is widely associated with anti-apoptotic functions.
- ERK can be anti-apoptotic by downregulating pro-apoptotic proteins and upregulating anti-apoptotic proteins.
- ERK1/2 signaling can be pro-apoptotic; cell cycle arrest and re-entry can induce apoptosis.
- ERK1/2 interacts with p53 and induces its phosphorylation, a mechanism of DNA damage-induced apoptosis.
- ERK1/2 activation contributes to the anti-proliferation and apoptotic effects of NSC 95397 in colon cancer cells.
An Easy Guide to Understand MAPKs-Regulated Apoptosis
- MAPKs must have signaling properties suited for determining cell survival/death.
Basic Signaling Properties of MAPKs
- MAPKs regulate cell fate decisions.
- Cellular sensors need properties for irreversible processes: Ultrasensitivity, Hysteresis, Digital Response.
- Positive and negative feedback loops are common regulatory elements.
- Ultrasensitive systems in positive feedback loops exhibit bistable behavior.
Strong Versus Weak and Sustained Versus Transient Signaling
- Ultrasensitive properties and threshold levels explain digital outputs obtained after activation.
- Strength and duration of signal regulate apoptosis.
- Transient JNK activation promotes survival, while prolonged JNK activation induces apoptosis.
- Duration of p38 phosphorylation is crucial; sustained activation is associated with apoptosis, transient with survival.
Feedback Loops
- Feedback loops are important to regulate intercellular signaling.
- Negative feedback loops maintain homeostasis and can produce oscillations.
- Positive feedback loops amplify signals and can create bistable switches.
How Cells Die through Positive Feedback Loops
- Ultrasensitive response and sustained activation result from positive feedback loops.
- Multiple positive feedback loops occur during cell death.
- Cytochrome c release induces caspase-9, promoting release and caspase-9/-3 activation.
- MEKK1 is cleaved by caspase-3, promoting caspase-9 activation.
- ROS regulates MAPK activation in a positive circuit.
Xenopus Oocytes as a Cell Model to Understand Apoptosis
- Xenopus oocytes are valuable for studying cell death mechanisms.
- They initiate the mitochondrial pathway of apoptosis.
- Unfertilized Xenopus eggs turn on the apoptotic machinery during meiotic maturation.
- Cytochrome c microinjection induces caspase-3 activity.
- Positive feedback loops allow apoptosis to spread in trigger waves.
MAPK Dynamics in Hyperosmotic Shock-Induced Apoptosis
- Hyperosmolarity damages cells, but cells adapt through survival mechanisms.
- Hyperosmotic stress induces cytochrome c release and caspase-3 activation.
- Simultaneous inhibition of p38 and JNK reduces osmostress-induced apoptosis.
- Caspases induce proteolysis of calpastatin, increasing calpain activation.
- A model for osmostress-induced apoptosis in Xenopus oocytes presents reversible and irreversible phases.
- MAPKs regulate apoptosis through transcriptional and post-transcriptional mechanisms.
- p38 and JNK are usually pro-apoptotic, and ERK is anti-apoptotic, but there are exceptions.
- MAPK signal crosstalk between JNK and p38 MAPK is an additional regulatory mechanism.
- The dual role of MAPKs is explained by diverse targets activated