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Literature summary for 2.7.1.107 extracted from

  • Kawasaki, T.; Kobayashi, T.; Ueyama, T.; Shirai, Y.; Saito, N.
    Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha (2008), Biochem. J., 409, 471-479.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in COS-7 cell and HeLa cell Homo sapiens

Protein Variants

Protein Variants Comment Organism
F369A/F372A significant decrease in diacylglycerol kinase activity. Mutant cells display reduced uptake of transferrin Homo sapiens
F369A/F372A/F748A significant decrease in diacylglycerol kinase activity. Mutant cells display reduced uptake of transferrin Homo sapiens
F748A diacylglycerol kinase activity similar to that of wild-type. Mutant cells display reduced uptake of transferrin Homo sapiens
additional information diacylglycerol kinase delta has alternative splicing variants, type 1 DGKdelta1 and type 2 DGKdelta2, with calculated molecular masses of 130 and 134 kDa, respectively. HeLa cells express both type 1 and 2 DGKdelta, and COS7 cells express only type 2 DGKdelta. In DGKdelta-knockdown cells uptake of transferrin is reduced. DGKdelta2 is partially co-localized with clathrin or adaptor protein AP2alpha in COS7 cells. Mutants lacking binding ability to AP2alpha as well as kinase-negative mutants cannot compensate for the uptake of transferrin inhibited by siRNA treatment. Overexpression of wild-type diacylglycerol kinase delta2 completely recovers the transferrin uptake Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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diacylglycerol kinase delta2
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Subunits

Subunits Comment Organism
More diacylglycerol kinase delta2 interacts with the platform subdomain of adaptor protein AP2alpha through its DXF-type binding motif. Binding is involved in the transferrin internalization Homo sapiens