Protein Variants | Comment | Organism |
---|---|---|
additional information | overexpression of these DAP5 truncates (45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments) demonstrates that DAP5-N retains the capability of initiating IRES-driven translation of apoptosis-associated p53, but not the prosurvival Bcl-2 (B-cell lymphoma 2) when compared with the full-length DAP5 | Coxsackievirus B3 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
death-associated protein 5 + H2O | Coxsackievirus B3 | DAP5 | ? | - |
? | |
eukaryotic translation initiation factor 4G + H2O | Coxsackievirus B3 | eIF4G | ? | - |
? | |
additional information | Coxsackievirus B3 | DAP5 is cleaved during CVB3 infection in tissue culture and in mouse heart | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Coxsackievirus B3 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
death-associated protein 5 + H2O | DAP5 | Coxsackievirus B3 | ? | - |
? | |
death-associated protein 5 + H2O | DAP5, generation of 45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments, respectively. DAP5 is cleaved at amino acid G434 | Coxsackievirus B3 | ? | - |
? | |
eukaryotic translation initiation factor 4G + H2O | eIF4G | Coxsackievirus B3 | ? | - |
? | |
additional information | DAP5 is cleaved during CVB3 infection in tissue culture and in mouse heart | Coxsackievirus B3 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
2A protease | - |
Coxsackievirus B3 |
coxsackievirus B3 2A protease | - |
Coxsackievirus B3 |
CVB3 2A | - |
Coxsackievirus B3 |
General Information | Comment | Organism |
---|---|---|
malfunction | overexpression of these DAP5 truncates (45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments) demonstrates that DAP5-N retains the capability of initiating IRES-driven translation of apoptosis-associated p53, but not the prosurvival Bcl-2 (B-cell lymphoma 2) when compared with the full-length DAP5 | Coxsackievirus B3 |
physiological function | death-associated protein 5 (DAP5) is cleaved during CVB3 infection by coxsackievirus B3 2A protease. Viral protease 2A but not 3C (EC 3.4.22.28) is responsible for DAP5 cleavage generating 45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments, respectively. Cleavage of DAP5 facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes. Also eukaryotic translation initiation factor 4G (eIF4G) is cleaved during infection by the enterovirus protease leading to the shutoff of cellular cap-dependent translation, but it does not affect the initiation of cap-independent translation of mRNAs containing an internal ribosome entry site (IRES). DAP5 is cleaved at amino acid G434. Upon cleavage, DAP5-N largely translocates to the nucleus at the later time points of infection, whereas the DAP5-C largely remains in the cytoplasm. DAP5-N expression promotes CVB3 replication and progeny release. On the other hand, DAP5-C exerts a dominant-negative effect on cap-dependent translation. DAP5 is cleaved into N- and C-terminal-truncated forms during CVB3 infection in vitro and in vivo and is transcriptionally downregulated. DAP5-N and DAP5-C differentially regulate translation of p53 and Bcl-2 and result in apoptotic cell death. DAP5-N and DAP5-C differentially alter translation but not transcription of IRES-containing genes p53 and Bcl-2 | Coxsackievirus B3 |