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Literature summary for 3.1.4.4 extracted from

  • Lee, J.S.; Kim, J.H.; Jang, I.H.; Kim, H.S.; Han, J.M.; Kazlauskas, A.; Yagisawa, H.; Suh, P.G.; Ryu, S.H.
    Phosphatidylinositol (3,4,5)-triphosphate specifically interacts with the phox homology domain of phospholipase D1 and stimulates its activity (2005), J. Cell Sci., 118, 4405-4413.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphatidylinositol 3,4,5-triphosphate specifically interacts with the phox homology domain of phospholipase D1 and stimulates activity Mus musculus

Protein Variants

Protein Variants Comment Organism
R179A mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate Mus musculus
R179K mutation disrupts binding of the activator phosphatidylinositol 3,4,5-triphosphate Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1 ?
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?

Organism

Organism UniProt Comment Textmining
Mus musculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
NIH-3T3 cell
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Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the PLD2 PX domain enables PLD1 to mediate signal transduction via ERK1/2 by providing a direct binding site for phosphatidylinositol 3,4,5-triphosphate and by activating PLD1 Mus musculus ?
-
?

Synonyms

Synonyms Comment Organism
phospholipase D1
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Mus musculus
PLD1
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Mus musculus