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Literature summary for 3.4.22.55 extracted from
- Caspase-2: the orphan caspase (2012), Cell Death Differ., 19, 51-57.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ATM/ATR | caspase-2 is activated by ATM/ATR independently of p53 when Chk1 activity is repressed | Mus musculus | |
| ATM/ATR | caspase-2 is activated by ATM/ATR independently of p53 when Chk1 activity is repressed | Homo sapiens | |
| additional information | caspase-2 is activated by dimerization | Mus musculus | |
| additional information | caspase-2 is activated by dimerization | Homo sapiens | |
| P53 | p53 induces PIDD expression resulting in a feed-forward loop | Mus musculus |  |
| P53 | p53 induces PIDD expression resulting in a feed-forward loop | Homo sapiens | |
| RAIDD | in response to cellular stresses, processed PIDD-CC binds to RAIDD in the cytoplasm, which recruits and activates caspase-2, overview | Mus musculus | |
| RAIDD | in response to cellular stresses, processed PIDD-CC binds to RAIDD in the cytoplasm, which recruits and activates caspase-2, overview | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| caspase-2 maps to the q34-35 segment of human chromosome 7 | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | - |
Mus musculus | 5737 | - |
| cytoplasm | - |
Homo sapiens | 5737 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Bid + H2O | Mus musculus | active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization | tBid + ? | - |
? | |
| Bid + H2O | Homo sapiens | active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization | tBid + ? | - |
? | |
| CUX1 + H2O | Mus musculus | - |
? | - |
? | |
| CUX1 + H2O | Homo sapiens | - |
? | - |
? | |
| golgin-160 + H2O | Mus musculus | - |
? | - |
? | |
| golgin-160 + H2O | Homo sapiens | - |
? | - |
? | |
| ICAD + H2O | Mus musculus | - |
? | - |
? | |
| ICAD + H2O | Homo sapiens | - |
? | - |
? | |
| MDM2 + H2O | Mus musculus | active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53 | MDM2 p60 + ? | - |
? | |
| MDM2 + H2O | Homo sapiens | active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53 | MDM2 p60 + ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Bid + H2O | active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization | Mus musculus | tBid + ? | - |
? | |
| Bid + H2O | active caspase-2 cleaves Bid to form tBid, which induces mitochondrial outer membrane permeabilization | Homo sapiens | tBid + ? | - |
? | |
| CUX1 + H2O | - |
Mus musculus | ? | - |
? | |
| CUX1 + H2O | - |
Homo sapiens | ? | - |
? | |
| golgin-160 + H2O | - |
Mus musculus | ? | - |
? | |
| golgin-160 + H2O | - |
Homo sapiens | ? | - |
? | |
| ICAD + H2O | - |
Mus musculus | ? | - |
? | |
| ICAD + H2O | - |
Homo sapiens | ? | - |
? | |
| MDM2 + H2O | active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53 | Mus musculus | MDM2 p60 + ? | - |
? | |
| MDM2 + H2O | active caspase-2 cleaves MDM2 to form MDM2 p60, which binds to and stabilizes p53 | Homo sapiens | MDM2 p60 + ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | caspase-2 is activated by dimerization, initiator caspases are present in the cell as inactive monomers and their activation is promoted by dimerization. Dimerization results when initiator caspases are recruited to large molecular weight protein complexes that act as signaling platforms | Mus musculus |
| dimer | caspase-2 is activated by dimerization, initiator caspases are present in the cell as inactive monomers and their activation is promoted by dimerization. Dimerization results when initiator caspases are recruited to large molecular weight protein complexes that act as signaling platforms | Homo sapiens |
| More | recruitment of caspase-2 to a higher molecular weight protein complex in cell extracts | Mus musculus |
| More | recruitment of caspase-2 to a higher molecular weight protein complex in cell extracts | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | caspase-2 knockout mice do not develop early spontaneous tumors, but loss of caspase-2 in mice is associated with accelerated tumorigenesis driven by transgenic c-Myc on the mu-enhancer, thus caspase-2-deficient embryonic fibroblasts are more efficiently transformed than wild-type cells. Caspase-2-deficient mice have features consistent with accelerated ageing, phenotype, overview | Mus musculus |
| malfunction | decreased caspase-2 and RAIDD expression is observed in mantle cell lymphoma tumor samples. In addition, drug resistance in childhood forms of acute lymphoblastic leukemia is correlated with decreased levels of caspase-2. In contrast, increased levels of caspase-2 in acute myelogenous leukemia and adult ALL are associated with decreased patient survival. Possibly inactivation of caspase-2 in tumors occurs through disruption of the pathway through mutation or improper regulation of a protein that regulates caspase-2 activity | Homo sapiens |
| physiological function | role of caspase-2 in apoptosis, and caspase-2 may act as a tumor suppressor, mechanisms through which caspase-2 signals, e.g. involving PIDD, also known as LRDD or leucine-rich repeat and death domain-containing protein, caspase-2 pathways to apoptosis and cell cycle arrest, detailed overview. PIDD activation and more importantly caspase-2 activation is not always synonymous with induction of apoptosis, a threshold of caspase-2 activation must be reached before caspase-2-dependent apoptosis is engaged. Cleavage of Mdm2 is not the sole way caspase-2 can induce growth arrest | Mus musculus |
| physiological function | role of caspase-2 in apoptosis, and caspase-2 may act as a tumor suppressor, mechanisms through which caspase-2 signals, e.g. involving PIDD, also known as LRDD or leucine-rich repeat and death domain-containing protein, caspase-2 pathways to apoptosis and cell cycle arrest, detailed overview. PIDD activation and more importantly caspase-2 activation is not always synonymous with induction of apoptosis, a threshold of caspase-2 activation must be reached before caspase-2-dependent apoptosis is engaged. Cleavage of Mdm2 is not the sole way caspase-2 can induce growth arrest | Homo sapiens |
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