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Literature summary for 2.7.1.107 extracted from

  • Baldanzi, G.; Cutrupi, S.; Chianale, F.; Gnocchi, V.; Rainero, E.; Porporato, P.; Filigheddu, N.; van Blitterswijk, W.J.; Parolini, O.; Bussolino, F.; Sinigaglia, F.; Graziani, A.
    Diacylglycerol kinase-alpha phosphorylation by Src on Y335 is required for activation, membrane recruitment and Hgf-induced cell motility (2008), Oncogene, 27, 942-956.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in COS-7 and HEK-293T cells Canis lupus familiaris

Protein Variants

Protein Variants Comment Organism
additional information deletion mutants lacking respectively the entire C-terminal half of diacylglycerol kinase alpha or the last 13 amino acids PPPRSTNFFGFLS. Contrary to wild-type, mutants are not pulled down by immobilized GST-Src-SH3 fusion protein Canis lupus familiaris
Y335F mutants is not tyrosine phosphorylated upon coexpression with activated Src mutant Y527F. Enzymatic activity is not stimulated by hepatocyte growth factor cell stimulation Canis lupus familiaris

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane recruitment of diacylglycerol kinase alpha to the membrane is mediated both via its proline-rich sequence and phosphorylation of Y335 Canis lupus familiaris 16020
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Organism

Organism UniProt Comment Textmining
Canis lupus familiaris
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein both hepatocytes growth factor stimulation and v-Src transformation induce tyrosine phosphorylation of diacylglycerol kinase alpha on Y335, through a mechanism requiring its proline-rich C-terminal sequence. Both proline-rich sequence and phosphorylation of Y335 mediate its enzymatic activation, its ability to interact respectively with SH3 and SH2 domains of Src, its recruitment to the membrane. Phosphorylation is required for hepatocyte growth factor-induced motility Canis lupus familiaris

Subunits

Subunits Comment Organism
More interaction with SH3 and SH2 domains of Src are mediated both via its proline-rich sequence and phosphorylation of Y335 Canis lupus familiaris