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Janus kinases (JAKs) belong to the family of non-receptor tyrosine kinases and are composed of four isoforms, JAK1, JAK2, JAK3, and TYK2, with up to 70% homology.307,308 JAK1, JAK2, and TYK2 are widely distributed in various tissues and cells, while JAK3 is only expressed in the bone marrow and lymphatic-derived cells.309 JAKs are able to transfer extracellular signals to the nucleus and mediate DNA transcription and protein expression.310 Receptor-coupled JAKs can be activated when inflammatory cytokines such as interleukin and interferon bind to cytokine receptors.311 Then JAKs catalyze the phosphorylation of receptor tyrosine residues and recruit and phosphorylate downstream signal transducer and activator of transcription (STAT) proteins. Activated STAT proteins promote their translocation to the nucleus and regulation of target-gene transcription and expression. Distinct cytoplasmic domains of cytokine receptors activate different JAKs and STATs.312 The JAK/STAT pathway runs downstream of more than 50 cytokines and growth factors and is considered to be the central communication node for the immune system.JA-7 Given the important role of the JAK/STAT pathway in cytokine signal transduction, targeting JAK/STAT is considered a promising strategy for the treatment of multiple autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus. Additionally, STAT signals (e.g., STAT3, STAT5, or STAT6) have been found to be frequently activated in malignant tumors, especially hematopoietic cancers and are involved in cell proliferation, survival, invasion, or inflammation.313 As the critical upstream protein of STAT signals, JAKs are also potential targets for cancer treatment. The application of JAK inhibitors in cancer is mainly focused on hematologic malignancies.314
Enhancer of zeste homolog 2 (EZH2), a histone methyltransferase, functions as a catalytic subunit of the polycomb repressor complex 2 (PRC2), which also comprises other members including embryonic ectoderm development (EED), suppressor of zeste 12 (SUZ12), and histone-binding proteins RbAp46/48.413 PRC2 is one of the two core complexes of polycomb group proteins (PcGs), and is responsible for transferring methyl groups from S-adenosyl-L-methionine (SAM) to lysine 27 on histone H3 (H3K27) through its C-terminal SET domain, resulting in chromatin compaction and transcriptional silencing of target genes. As the central component of PRC2, EZH2 is involved in numerous epigenetic modifications that are associated with cell proliferation, differentiation, survival, adhesion, and DNA damage repair.414 Dysfunction of EZH2 is closely related to tumorigenesis and progression. Accumulating evidence has confirmed that EZH2 is frequently mutated and abnormally overexpressed in various malignant tumors including prostate cancer,415,416 ovarian cancer,417 endometrial carcinoma,418 breast cancer,419 melanoma as well as hematological malignancies,420 such as NHL, B-cell lymphoma, and T-cell ALL.421,422,423,424 It promotes tumorigenesis mainly through three mechanisms: PRC2-dependent H3K27 methylation, PRC2-dependent non-histone protein methylation, and PRC2-independent coactivator of transcriptional factors. Given the evidence for EZH2 enzymatic gain of function being a cancer driver, inhibition of EZH2 has been thought of as a novel and promising approach for cancer therapy.413
Schematic illustration of extrinsic and intrinsic pathways of apoptosis. In healthy cells, anti-apoptotic BCL-2 proteins (BCL-2, BCL-XL, BCL-W, MCL-1, and A1/BFL-1) bind to and inhibit activators (BH3-only proteins) and effectors (BAX and BAK). Treatment with BCL-2 inhibitors releases the inhibitory effects of anti-apoptotic BCL-2 proteins on activators and effectors. The subsequent activation and oligomerization of the pro-apoptotic proteins BAK and BAX result in the formation of mitochondrial outer membrane permeabilization (MOMP) and the release of cytochrome C as well as a second mitochondria-derived activator of caspase (SMAC) from the mitochondria. Cytochrome C can form a complex with procaspase 9 and apoptosis protease-activating factor 1 (APAF1), thereby activating caspase 9. Caspase 9 then activates procaspase 3 and procaspase 7, resulting in cell apoptosis. Figure created with BioRender.com
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FIGURE 3. Manipulation of ISR in cancer therapy. ATF4 induction can be achieved either through kinase activators such as bortezomib, gemcitabline, lopinavir, CCT020312, halofuginone, arginine deiminase, STAT3 inhibitors, BEPP, BTdCPU and ONC201 or the inhibitors of phosphatases such as salubrinal, guanabenz and nelfinavir. In the case of ISR promotes cancer cell survival and resistant to therapeutic treatments, inhibition of ATF4 can be achieved by kinase inhibitors such as LY-4, GSK2606414, AMG-44, BCR-ABL inhibitors, SP600125, C16 and aminopyranzolindane or compound ISRIB downstream of eIF2α phosphorylation.
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