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Literature summary for 4.4.1.14 extracted from

  • Kamiyoshihara, Y.; Iwata, M.; Fukaya, T.; Tatsuki, M.; Mori, H.
    Turnover of LeACS2, a wound-inducible 1-aminocyclopropane-1-carboxylic acid synthase in tomato, is regulated by phosphorylation/dephosphorylation (2010), Plant J., 64, 140-150.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Solanum lycopersicum

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum P18485 isoform ACS2
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation/dephosphorylation of ACS2 regulates its turnover upstream of the ubiquitin-26S-proteasome degradation pathway. ACS2 is stabilized by phosphorylation and degraded after dephosphorylation. The amount of ACS2 affected by the protein kinase/phosphatase inhibitors significantly influences cellular ACS activity, 1-aminocyclopropane-1-carboxylic acid content, and ethylene production levels in tomato fruit tissue. Calcium-dependent protein kinase CDPK2, is one of the protein kinases that are able to phosphorylate ACS2 at residue S460. ACS2 is immediately phosphorylated after translation by CDPK and mitogen-activated protein kinase at different sites in response to wound signaling and almost all functional ACS2 molecules are phosphorylated in the cell. Phosphorylation at both sites is required for ACS2 stability Solanum lycopersicum

Source Tissue

Source Tissue Comment Organism Textmining
fruit
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Solanum lycopersicum
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Synonyms

Synonyms Comment Organism
ACS2
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Solanum lycopersicum

General Information

General Information Comment Organism
metabolism phosphorylation/dephosphorylation of ACS2 regulates its turnover upstream of the ubiquitin-26S-proteasome degradation pathway. ACS2 is stabilized by phosphorylation and degraded after dephosphorylation. The amount of ACS2 affected by the protein kinase/phosphatase inhibitors significantly influences cellular ACS activity, 1-aminocyclopropane-1-carboxylic acid content, and ethylene production levels in tomato fruit tissue. Calcium-dependent protein kinase CDPK2, is one of the protein kinases that are able to phosphorylate ACS2 at residue S460. ACS2 is immediately phosphorylated after translation by CDPK and mitogen-activated protein kinase at different sites in response to wound signaling and almost all functional ACS2 molecules are phosphorylated in the cell. Phosphorylation at both sites is required for ACS2 stability Solanum lycopersicum