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Caspase-9: structure, mechanisms and clinical application

Li, Ping, Zhou, Libin, Zhao, Ting, Liu, Xiongxiong, Zhang, Pengcheng, Liu, Yan, Zheng, Xiaogang, Li, Qiang·2017·Oncotarget
DOI 10.18632/oncotarget.15098PMC PMC5410359
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Figure 1 The diagram of human caspase-9 A. Exons are numbered inside the boxes and their lengths are shown on top. B. The predicted amino acid structure is depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes. The three major domains are shaded: the pro-domain (within which the CARD domain is located, also called adaptor domain), the large subunit catalytic domain (LSCD), as well as the small subunit catalytic domain (SSCD, both LSCD and SSCD are also called catalytic domain). The linker domain (LD) is also indicated. The location of amino acid residues involved in the proteolytic processing of the procaspase-9 molecule is shown as well as the sites targeted for post-translational modification.
Figure 1 The diagram of human caspase-9 A. Exons are numbered inside the boxes and their lengths are shown on top. B. The predicted amino acid structure is depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes. The three major domains are shaded: the pro-domain (within which the CARD domain is located, also called adaptor domain), the large subunit catalytic domain (LSCD), as well as the small subunit catalytic domain (SSCD, both LSCD and SSCD are also called catalytic domain). The linker domain (LD) is also indicated. The location of amino acid residues involved in the proteolytic processing of the procaspase-9 molecule is shown as well as the sites targeted for post-translational modification.CC BY · PubMed Central
Figure 2 Regulation of caspase-9 by endogenous regulators in different signalling pathways Following cytochrome c release from mitochondria, a heptameric wheel-like multimeric complex, the apoptosome, induced and composed by Apaf-1 and procaspase-9. Factors such as ATP, can inhibit this process by directly inhibiting the interaction between Apaf-1 and cytochrome c. Recruitment of procaspase-9 to the apoptosome is antagonized by TUNCAN, and stimulated by NAC/DEFCAP. HAX-1 may inhibit caspase-9 activation, thereby suppressing apoptosis in cardiac myocytes. Direct phosphorylation at Thr125 by ERK1/2 (growth/survival signals), CDK1-cyclin B1 (in mitosis), p38αMAPK (upon hyperosmotic stress) and DYRK1A (in development and upon hyperosmotic stress) inhibits caspase-9 activity. PKCξ also inhibits phosphorylation of caspase-9 at Ser144 induced by hyperosmotic stress. Akt/PKB, as a protein kinase, suppresses the activation of caspase-9 in response to extracellular growth/survival signals. The interactions of HBIXP and XIAP with survivin block the activation of caspase-9 through distinct mechanisms. PKA seems to block the recruitment of caspase-9 to apoptosome rather than inhibitory effect on caspase-9 activation (unclear). CK2 phosphorylates caspase-9 at Ser348 to protect from caspase-8 cleavage in mouse, but not conserved in humans. Nitrosylation of caspase-9 by the donor of NO suggests cleavage inhibition of procaspase-9 and consequently apoptosis. Conversely, phosphorylation at Tyr153 by c-Abl stimulates activiation of caspase-9. Nucling recruits and transports the apoptosome when responding to the apoptosis induced by stresses. See text for more details.
Figure 2 Regulation of caspase-9 by endogenous regulators in different signalling pathways Following cytochrome c release from mitochondria, a heptameric wheel-like multimeric complex, the apoptosome, induced and composed by Apaf-1 and procaspase-9. Factors such as ATP, can inhibit this process by directly inhibiting the interaction between Apaf-1 and cytochrome c. Recruitment of procaspase-9 to the apoptosome is antagonized by TUNCAN, and stimulated by NAC/DEFCAP. HAX-1 may inhibit caspase-9 activation, thereby suppressing apoptosis in cardiac myocytes. Direct phosphorylation at Thr125 by ERK1/2 (growth/survival signals), CDK1-cyclin B1 (in mitosis), p38αMAPK (upon hyperosmotic stress) and DYRK1A (in development and upon hyperosmotic stress) inhibits caspase-9 activity. PKCξ also inhibits phosphorylation of caspase-9 at Ser144 induced by hyperosmotic stress. Akt/PKB, as a protein kinase, suppresses the activation of caspase-9 in response to extracellular growth/survival signals. The interactions of HBIXP and XIAP with survivin block the activation of caspase-9 through distinct mechanisms. PKA seems to block the recruitment of caspase-9 to apoptosome rather than inhibitory effect on caspase-9 activation (unclear). CK2 phosphorylates caspase-9 at Ser348 to protect from caspase-8 cleavage in mouse, but not conserved in humans. Nitrosylation of caspase-9 by the donor of NO suggests cleavage inhibition of procaspase-9 and consequently apoptosis. Conversely, phosphorylation at Tyr153 by c-Abl stimulates activiation of caspase-9. Nucling recruits and transports the apoptosome when responding to the apoptosis induced by stresses. See text for more details.CC BY · PubMed Central
Figure 3 Alternative splice variants of human caspase-9 A. Nucleotide alignment of human caspase-9a with caspase-9b. The bases marked with red color show the identical sequence of both caspase-9a and caspase-9b while the single-line bases in black color represent the alternative splicing sites. The alignment is processed by the online multiple-sequence alignment software MultAlin. B. Deduced structural comparison of the human caspase-9a and caspase-9b is presented. The two sequences refer to the Refseq. NM_001229.4 (caspase-9a) and NM_001278054.1 (caspase-9b). As indicated in the diagram, caspase-9b/9S lacks the entire large subunit catalytic domain (LSCD) found in the full-length protein. The aligned amino acid sequences are depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes.
Figure 3 Alternative splice variants of human caspase-9 A. Nucleotide alignment of human caspase-9a with caspase-9b. The bases marked with red color show the identical sequence of both caspase-9a and caspase-9b while the single-line bases in black color represent the alternative splicing sites. The alignment is processed by the online multiple-sequence alignment software MultAlin. B. Deduced structural comparison of the human caspase-9a and caspase-9b is presented. The two sequences refer to the Refseq. NM_001229.4 (caspase-9a) and NM_001278054.1 (caspase-9b). As indicated in the diagram, caspase-9b/9S lacks the entire large subunit catalytic domain (LSCD) found in the full-length protein. The aligned amino acid sequences are depicted with the translated regions marked with different colors. Exon regions transcribed but not translated are depicted as white boxes.CC BY · PubMed Central
Figure 4 The apoptosis of transduced cells incurred by activated iCasp9 A. iCasp9 is formed by connecting a drug-binding domain, FKBP12-F36V with Δcaspase9 via a SGGGS linker. Binding of small CID (AP1903 or AP20187) leads to dimerization of iCas9, thereby relaying activation signals and initiating mitochondrial apoptosis pathway. B. The bicistronic transgene, iCaps9.2A.ΔCD19, comprises iCasp9 sequence, linked via a short 2A-like sequence, with truncated CD19 using as a selectable marker.
Figure 4 The apoptosis of transduced cells incurred by activated iCasp9 A. iCasp9 is formed by connecting a drug-binding domain, FKBP12-F36V with Δcaspase9 via a SGGGS linker. Binding of small CID (AP1903 or AP20187) leads to dimerization of iCas9, thereby relaying activation signals and initiating mitochondrial apoptosis pathway. B. The bicistronic transgene, iCaps9.2A.ΔCD19, comprises iCasp9 sequence, linked via a short 2A-like sequence, with truncated CD19 using as a selectable marker.CC BY · PubMed Central

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Authors
Li, P., Zhou, L., Zhao, T., Liu, X., Zhang, P., Liu, Y., Zheng, X., & Li, Q.
Venue
Oncotarget
Publisher
Impact Journals, LLC
Published
2017-02-04
Volume
8
Issue
14
Pages
23996-24008
ISSN
1949-2553
DOI
10.18632/oncotarget.15098
PMC
PMC5410359
Cited by
319
References
1
Language
en

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