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PMID: 17905508 those with a short prodomain (procaspase-3, -6 and -7) exist in the cells as dimers that require proteolysis at internal aspartate residues to generate two large and two small subunits whose heterodimerization forms the active enzyme. Indirect PMID: 17905508 Activation of specific caspases in response to Epo in erythroid precursors leads to the specific cleavage of cellular targets such as PARP1, Acinus and Lamin B whereas the key differentiation- involved transcription factor GATA-1 is protected from cleavage by HSP70. PMID: 17905508 The RIP1 cleavage generates a fragment that prevents the sustained activation of NF-kappaB, which is observed in monocytes undergoing differentiation into dendritic cells, and contributes to the down-regulation of NF-kappaB that characterizes the differentiation of monocytes into macrophage. PMID: 17905508 The growth factor M-CSF/CSF-1 is a disulfide-linked homodimer that binds to CSF-1 receptor, stabilizes its non-covalent dimerization, activates its kinase activity and stimulates its tyrosine phosphorylation. PMID: 17905508, 17047155 In response to M-CSF/CSF-1, procaspase-8 interacts with the adaptor molecule FADD (Fas- Associated Death Domain), the serine threonine kinase RIP1 and the long and short isoforms of FLIP. PMID: 17905508, 12966146 This limited phosphorylation induces the covalent dimerization of the receptor through disulfide binding, which activates a second wave of tyrosine phosphorylation of the receptor and its interaction with downstream signaling molecules that include phosphatidylinositol- 3-kinases, extracellular-signal-related kinases and Src kinases. PMID: 17905508, 8343951 The binding of one Epo molecule to its receptor, which exists as a preformed dimer or dimerizes upon Epo binding, induces a conformational change that activated the constitutively associated JAK2 (Janus family tyrosine protein kinase 2) by transphosphorylation. PMID: 17905508 Epo starvation induces Hsp70 nucleus export and exposes GATA-1 to caspase-mediated cleavage. Indirect PMID: 17905508, 16636047 This approach, performed in the U937 cell line model, identified several proteins whose caspase-mediated cleavage was confirmed in primary monocytes exposed to M-CSF. These target proteins include p21-activated kinase-2, Nucleophosmin, a-Tubulin, Vinculin, Plasminogen Activator Inhibitory-2 (PAI-2), and several proteins of the hnRNP family. PMID: 17905508 One of the soluble molecules subsequently released in the cytosol is cytochrome c, which induces Apaf-1 (apoptotic protease-activating factor 1) oligomerization and procaspase-9 recruitment and activation in the so-called apoptosome. PMID: 17905508, 17047155 In response to M-CSF/CSF-1, procaspase-8 interacts with the adaptor molecule FADD (Fas- Associated Death Domain), the serine threonine kinase RIP1 and the long and short isoforms of FLIP. PMID: 17905508 In turn, JAK2 molecules phosphorylate the eight tyrosine residues in the cytoplasmic domain of the Epo receptor, which then serve as docking sites for signaling molecules that contain Src homology 2 (SH2) domains such as STAT5 (Signal Transducer and Activator of Transcription 5), leading to its homodimerization and activation through phosphorylation. Indirect PMID: 17905508 Activation of specific caspases in response to Epo in erythroid precursors leads to the specific cleavage of cellular targets such as PARP1, Acinus and Lamin B whereas the key differentiation- involved transcription factor GATA-1 is protected from cleavage by HSP70. Indirect PMID: 17905508, 14976035, 12438425, 11208865 Caspase-3, together with caspase-9, -7 and -2, are transiently activated during erythroid differentiation induced by Epo and caspase inhibition completely inhibits erythroid differentiation at the basophilic erythroblast stage. PMID: 17905508 those with a short prodomain (procaspase-3, -6 and -7) exist in the cells as dimers that require proteolysis at internal aspartate residues to generate two large and two small subunits whose heterodimerization forms the active enzyme. PMID: 17905508 Interaction of a death receptor such as Fas (CD95), with its ligand, triggers formation of a death-inducing signaling complex (DISC), including the adaptor molecule FADD, which in turn recruits procaspase-8. PMID: 17905508 Interaction of a death receptor such as Fas (CD95), with its ligand, triggers formation of a death-inducing signaling complex (DISC), including the adaptor molecule FADD, which in turn recruits procaspase-8. PMID: 17905508 One of the soluble molecules subsequently released in the cytosol is cytochrome c, which induces Apaf-1 (apoptotic protease-activating factor 1) oligomerization and procaspase-9 recruitment and activation in the so-called apoptosome. PMID: 17905508 Caspase-8 is activated in response to M-CSF that induces the formation of a multimolecular platform in which FADD, RIP1 and FLIP were identified. PMID: 17905508 Along erythroid differentiation, activated caspase-3 and, to a lower extent, caspase-7, are found in the nucleus where they co-localize with GATA-1 but this transcription factor is protected from caspase-mediated proteolysis through interaction with the chaperone heat shock protein Hsp70. Indirect PMID: 17905508, 16636047 This approach, performed in the U937 cell line model, identified several proteins whose caspase-mediated cleavage was confirmed in primary monocytes exposed to M-CSF. These target proteins include p21-activated kinase-2, Nucleophosmin, a-Tubulin, Vinculin, Plasminogen Activator Inhibitory-2 (PAI-2), and several proteins of the hnRNP family. Indirect PMID: 17905508 Other active signaling molecules recruited by the phosphorylated Epo receptor include the phopshatidylinositol- 3 kinase that, together with STAT5, promote erythroid cell survival, and son of sevenless protein recruited through the adaptor protein Grb-2 to activate the RAS/MAP (mitogen- activated protein) kinase pathway, thereby promoting proliferation. PMID: 17905508 Along erythroid differentiation, activated caspase-3 and, to a lower extent, caspase-7, are found in the nucleus where they co-localize with GATA-1 but this transcription factor is protected from caspase-mediated proteolysis through interaction with the chaperone heat shock protein Hsp70. PMID: 17905508 Procaspase-8 is then activated by proximity-induced dimerization within this oligomeric recruitment complex, which in turn activates the caspase cascade. PMID: 17905508, 12966146 This limited phosphorylation induces the covalent dimerization of the receptor through disulfide binding, which activates a second wave of tyrosine phosphorylation of the receptor and its interaction with downstream signaling molecules that include phosphatidylinositol- 3-kinases, extracellular-signal-related kinases and Src kinases. Indirect PMID: 17905508, 16636047 This approach, performed in the U937 cell line model, identified several proteins whose caspase-mediated cleavage was confirmed in primary monocytes exposed to M-CSF. These target proteins include p21-activated kinase-2, Nucleophosmin, a-Tubulin, Vinculin, Plasminogen Activator Inhibitory-2 (PAI-2), and several proteins of the hnRNP family. PMID: 17905508, 8343951 The binding of one Epo molecule to its receptor, which exists as a preformed dimer or dimerizes upon Epo binding, induces a conformational change that activated the constitutively associated JAK2 (Janus family tyrosine protein kinase 2) by transphosphorylation. Indirect PMID: 17905508 Activation of specific caspases in response to Epo in erythroid precursors leads to the specific cleavage of cellular targets such as PARP1, Acinus and Lamin B whereas the key differentiation- involved transcription factor GATA-1 is protected from cleavage by HSP70. Indirect PMID: 17905508 PAK-2 can be activated by the monomeric G proteins Cdc42 and Rac that, in their GTP-bound state, bind to a conserved region within the Nterminal domain of PAKs to release inhibition of the catalytic site by an overlapping autoinhibitory domain. PMID: 17905508 A cleavage fragment of RIP1, generated by active caspase-8, contributes to the down-regulation of NF-kappaB whereas caspase-3, activated downstream of caspase-8, cleaves other target proteins such as PAK2 and nucleophosmin that contribute to the differentiation. PMID: 17905508 In turn, JAK2 molecules phosphorylate the eight tyrosine residues in the cytoplasmic domain of the Epo receptor, which then serve as docking sites for signaling molecules that contain Src homology 2 (SH2) domains such as STAT5 (Signal Transducer and Activator of Transcription 5), leading to its homodimerization and activation through phosphorylation. PMID: 17905508 The growth factor M-CSF/CSF-1 is a disulfide-linked homodimer that binds to CSF-1 receptor, stabilizes its non-covalent dimerization, activates its kinase activity and stimulates its tyrosine phosphorylation. PMID: 17905508 those with a short prodomain (procaspase-3, -6 and -7) exist in the cells as dimers that require proteolysis at internal aspartate residues to generate two large and two small subunits whose heterodimerization forms the active enzyme. PMID: 17905508 Other active signaling molecules recruited by the phosphorylated Epo receptor include the phopshatidylinositol- 3 kinase that, together with STAT5, promote erythroid cell survival, and son of sevenless protein recruited through the adaptor protein Grb-2 to activate the RAS/MAP (mitogen- activated protein) kinase pathway, thereby promoting proliferation. Indirect PMID: 17905508 those with a short prodomain (procaspase-3, -6 and -7) exist in the cells as dimers that require proteolysis at internal aspartate residues to generate two large and two small subunits whose heterodimerization forms the active enzyme. PMID: 17905508, 14976035, 12438425, 11208865 Caspase-3, together with caspase-9, -7 and -2, are transiently activated during erythroid differentiation induced by Epo and caspase inhibition completely inhibits erythroid differentiation at the basophilic erythroblast stage. PMID: 17905508, 12966146 This limited phosphorylation induces the covalent dimerization of the receptor through disulfide binding, which activates a second wave of tyrosine phosphorylation of the receptor and its interaction with downstream signaling molecules that include phosphatidylinositol- 3-kinases, extracellular-signal-related kinases and Src kinases. PMID: 17905508 Along erythroid differentiation, activated caspase-3 and, to a lower extent, caspase-7, are found in the nucleus where they co-localize with GATA-1 but this transcription factor is protected from caspase-mediated proteolysis through interaction with the chaperone heat shock protein Hsp70. PMID: 17905508, 12966146 This limited phosphorylation induces the covalent dimerization of the receptor through disulfide binding, which activates a second wave of tyrosine phosphorylation of the receptor and its interaction with downstream signaling molecules that include phosphatidylinositol- 3-kinases, extracellular-signal-related kinases and Src kinases. Indirect PMID: 17905508 One of the soluble molecules subsequently released in the cytosol is cytochrome c, which induces Apaf-1 (apoptotic protease-activating factor 1) oligomerization and procaspase-9 recruitment and activation in the so-called apoptosome. Indirect PMID: 17905508, 14976035, 12438425, 11208865 Caspase-3, together with caspase-9, -7 and -2, are transiently activated during erythroid differentiation induced by Epo and caspase inhibition completely inhibits erythroid differentiation at the basophilic erythroblast stage. PMID: 17905508 Interaction of a death receptor such as Fas (CD95), with its ligand, triggers formation of a death-inducing signaling complex (DISC), including the adaptor molecule FADD, which in turn recruits procaspase-8. Indirect PMID: 17905508, 10359572, 10428030 In Epo-deprived as well as Fas-ligand treated immature erythroblasts, activated caspases cleave the transcription factor GATA-1. This transcription factor mediates Epo-induced up-regulation of the anti-apoptotic protein Bcl-XL. PMID: 17905508 In turn, JAK2 molecules phosphorylate the eight tyrosine residues in the cytoplasmic domain of the Epo receptor, which then serve as docking sites for signaling molecules that contain Src homology 2 (SH2) domains such as STAT5 (Signal Transducer and Activator of Transcription 5), leading to its homodimerization and activation through phosphorylation. Indirect PMID: 17905508, 10359572, 10428030 In Epo-deprived as well as Fas-ligand treated immature erythroblasts, activated caspases cleave the transcription factor GATA-1. This transcription factor mediates Epo-induced up-regulation of the anti-apoptotic protein Bcl-XL. PMID: 17905508, 14976035, 12438425, 11208865 Caspase-3, together with caspase-9, -7 and -2, are transiently activated during erythroid differentiation induced by Epo and caspase inhibition completely inhibits erythroid differentiation at the basophilic erythroblast stage. Indirect PMID: 17905508 PAK-2 can be activated by the monomeric G proteins Cdc42 and Rac that, in their GTP-bound state, bind to a conserved region within the Nterminal domain of PAKs to release inhibition of the catalytic site by an overlapping autoinhibitory domain. PMID: 17905508 Interestingly, RIP1 is cleaved by caspase-8 in the multimolecular platform. PMID: 17905508, 17047155, 12393560 We also observed that another well identified caspase target, Lamin B, remained uncleaved whereas three other caspase targets, namely RIP1, FLIP and Acinus, were cleaved. PMID: 17905508, 8343951 The binding of one Epo molecule to its receptor, which exists as a preformed dimer or dimerizes upon Epo binding, induces a conformational change that activated the constitutively associated JAK2 (Janus family tyrosine protein kinase 2) by transphosphorylation. Indirect PMID: 17905508 Other active signaling molecules recruited by the phosphorylated Epo receptor include the phopshatidylinositol- 3 kinase that, together with STAT5, promote erythroid cell survival, and son of sevenless protein recruited through the adaptor protein Grb-2 to activate the RAS/MAP (mitogen- activated protein) kinase pathway, thereby promoting proliferation. Indirect PMID: 17905508 A cleavage fragment of RIP1, generated by active caspase-8, contributes to the down-regulation of NF-kappaB whereas caspase-3, activated downstream of caspase-8, cleaves other target proteins such as PAK2 and nucleophosmin that contribute to the differentiation. PMID: 17905508, 8343951 The binding of one Epo molecule to its receptor, which exists as a preformed dimer or dimerizes upon Epo binding, induces a conformational change that activated the constitutively associated JAK2 (Janus family tyrosine protein kinase 2) by transphosphorylation. Indirect PMID: 17905508, 10359572, 10428030 In Epo-deprived as well as Fas-ligand treated immature erythroblasts, activated caspases cleave the transcription factor GATA-1. This transcription factor mediates Epo-induced up-regulation of the anti-apoptotic protein Bcl-XL. PMID: 17905508 In turn, JAK2 molecules phosphorylate the eight tyrosine residues in the cytoplasmic domain of the Epo receptor, which then serve as docking sites for signaling molecules that contain Src homology 2 (SH2) domains such as STAT5 (Signal Transducer and Activator of Transcription 5), leading to its homodimerization and activation through phosphorylation. PMID: 17905508 Other active signaling molecules recruited by the phosphorylated Epo receptor include the phopshatidylinositol- 3 kinase that, together with STAT5, promote erythroid cell survival, and son of sevenless protein recruited through the adaptor protein Grb-2 to activate the RAS/MAP (mitogen- activated protein) kinase pathway, thereby promoting proliferation. PMID: 17905508 Other active signaling molecules recruited by the phosphorylated Epo receptor include the phopshatidylinositol- 3 kinase that, together with STAT5, promote erythroid cell survival, and son of sevenless protein recruited through the adaptor protein Grb-2 to activate the RAS/MAP (mitogen- activated protein) kinase pathway, thereby promoting proliferation. PMID: 17905508 Procaspase-8 is then activated by proximity-induced dimerization within this oligomeric recruitment complex, which in turn activates the caspase cascade. Indirect Indirect PMID: 17905508 those with a short prodomain (procaspase-3, -6 and -7) exist in the cells as dimers that require proteolysis at internal aspartate residues to generate two large and two small subunits whose heterodimerization forms the active enzyme. PMID: 17905508, 14976035, 12438425, 11208865 Caspase-3, together with caspase-9, -7 and -2, are transiently activated during erythroid differentiation induced by Epo and caspase inhibition completely inhibits erythroid differentiation at the basophilic erythroblast stage. Indirect PMID: 17905508 In the presence of Epo, Hsp70 migrates in the nucleus when caspases are activated and protect GATA-1 from caspase-mediated cleavage.