Title : Phospholipase D is associated in a phorbol ester-dependent manner with protein kinase C-alpha and with a 220-kDa protein which is phosphorylated on serine and threonine.

Pub. Date : 1998 Jul 30

PMID : 9703960






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 In this study, a PLD isoform (rPLD1) was shown to bind to PKC-alpha in Rat1 fibroblasts treated with phorbol ester. Phorbol Esters phospholipase D1 Rattus norvegicus
2 p220 was phosphorylated on serine/threonine in PMA-stimulated Rat1 cells, and rPLD1 expressed in Sf9 cells was also serine/threonine phosphorylated in response to PMA treatment. Serine phospholipase D1 Rattus norvegicus
3 p220 was phosphorylated on serine/threonine in PMA-stimulated Rat1 cells, and rPLD1 expressed in Sf9 cells was also serine/threonine phosphorylated in response to PMA treatment. Threonine phospholipase D1 Rattus norvegicus
4 These data suggest the PMA induces the formation of a RPLD1/PKC alpha/P220 complex in cells, some components of which undergo serine/threonine phosphorylation. Serine phospholipase D1 Rattus norvegicus
5 These data suggest the PMA induces the formation of a RPLD1/PKC alpha/P220 complex in cells, some components of which undergo serine/threonine phosphorylation. Threonine phospholipase D1 Rattus norvegicus