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Literature summary for 3.4.22.29 extracted from

  • Hanson, P.J.; Ye, X.; Qiu, Y.; Zhang, H.M.; Hemida, M.G.; Wang, F.; Lim, T.; Gu, A.; Cho, B.; Kim, H.; Fung, G.; Granville, D.J.; Yang, D.
    Cleavage of DAP5 by coxsackievirus B3 2A protease facilitates viral replication and enhances apoptosis by altering translation of IRES-containing genes (2016), Cell Death Differ., 23, 828-840 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.29

Protein Variants

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Coxsackievirus B3
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-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
2A protease
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 Coxsackievirus B3
coxsackievirus B3 2A protease
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 Coxsackievirus B3
CVB3 2A
-
 Coxsackievirus B3

General Information

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