ArticleThe Biochemical journal2001
Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 108 citations in OpenAlex.
- Caspase-5: Structure, Pro-Inflammatory Activity and Evolution.Biomolecules · 2024Review
- CK2 and the Hallmarks of Cancer.Biomedicines · 2022Review
- Great balls of fire: activation and signalling of inflammatory caspases.Biochemical Society transactions · 2021Review
- Evaluation of the effects of phosphorylation of synthetic peptide substrates on their cleavage by caspase-3 and -7.The Biochemical journal · 2021Article
- Synthesis of Novel Halogenated Heterocycles Based onMolecules (Basel, Switzerland) · 2021Article
- Cell-Cycle Cross Talk with Caspases and Their Substrates.Cold Spring Harbor perspectives in biology · 2020Review
- Interaction between caspase-3 and caspase-5 in the stretch-induced programmed cell death in the human periodontal ligament cells.Journal of cellular physiology · 2019Article
- Processing and secretion of guanylate binding protein-1 depend on inflammatory caspase activity.Journal of cellular and molecular medicine · 2017Article
- The Phosphorylation of PDX-1 by Protein Kinase CK2 Is Crucial for Its Stability.Pharmaceuticals (Basel, Switzerland) · 2016Article
- Cacidases: caspases can cleave after aspartate, glutamate and phosphoserine residues.Cell death and differentiation · 2016Article
- Article
- The interaction of MYC with the trithorax protein ASH2L promotes gene transcription by regulating H3K27 modification.Nucleic acids research · 2014Article
- Regulation of the proapoptotic functions of prostate apoptosis response-4 (Par-4) by casein kinase 2 in prostate cancer cells.Cell death & disease · 2014Article
- Inhibition of MAPKs, Myc/Max, NFκB, and hypoxia pathways by Phyllanthus prevents proliferation, metastasis and angiogenesis in human melanoma (MeWo) cancer cell line.International journal of medical sciences · 2014Article
- Article
- Phosphorylation of the transcription factor YY1 by CK2α prevents cleavage by caspase 7 during apoptosis.Molecular and cellular biology · 2012Article
- Regulation of caspase pathways by protein kinase CK2: identification of proteins with overlapping CK2 and caspase consensus motifs.Molecular and cellular biochemistry · 2011Article
- Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro.Cell cycle (Georgetown, Tex.) · 2011Article
- Impact of protein kinase CK2 on inhibitor of apoptosis proteins in prostate cancer cells.Molecular and cellular biochemistry · 2008Article
- Phosphorylation of murine caspase-9 by the protein kinase casein kinase 2 regulates its cleavage by caspase-8.The Journal of biological chemistry · 2008Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Max is the central component of the Myc/Max/Mad network of transcription factors that regulate growth, differentiation and apoptosis. Whereas the Myc and Mad genes and proteins are highly regulated, Max expression is constitutive and no post-translational regulation is known. We have found that Max is targeted during Fas-induced apoptosis. Max is first dephosphorylated and subsequently cleaved by caspases. Two specific cleavage sites for caspases in Max were identified, one at IEVE(10) decreasing S and one at SAFD(135) decreasing G near the C-terminus, which are cleaved in vitro by caspase-5 and caspase-7 respectively. Mutational analysis indicates that both sites are also used in vivo. Thus Max represents the first caspase-5 substrate. The unusual cleavage after a glutamic acid residue is observed only with full-length, DNA-binding competent Max protein but not with corresponding peptides, suggesting that structural determinants might be important for this activity. Furthermore, cleavage by caspase-5 is inhibited by the protein kinase CK2-mediated phosphorylation of Max at Ser-11, a previously mapped phosphorylation site in vivo. These findings suggest that Fas-mediated dephosphorylation of Max is required for cleavage by caspase-5. The modifications that occur on Max in response to Fas signalling affect the DNA-binding activity of Max/Max homodimers. Taken together, our findings uncover three distinct processes, namely dephosphorylation and cleavage by caspase-5 and caspase-7, that target Max during Fas-mediated apoptosis, suggesting the regulation of the Myc/Max/Mad network through its central component.
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