Title : Phospholipase D1 in caveolae: regulation by protein kinase Calpha and caveolin-1.

Pub. Date : 1999 Mar 23

PMID : 10090765






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate protein kinase C, alpha Rattus norvegicus
2 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate protein kinase C, alpha Rattus norvegicus
3 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate protein kinase C, alpha Rattus norvegicus
4 Previously we have demonstrated that protein kinase Calpha (PKCalpha) directly interacts with phospholipase D1 (PLD1), activating the enzymatic activity of PLD1 in the presence of phorbol 12-myristate 13-acetate (PMA) [Lee, T. G., et al. Tetradecanoylphorbol Acetate protein kinase C, alpha Rattus norvegicus
5 PMA elicits translocation of PKCalpha to the CEMs, inducing PLD activation through the interaction of PKCalpha with PLD1 in the CEMs. Tetradecanoylphorbol Acetate protein kinase C, alpha Rattus norvegicus
6 PMA elicits translocation of PKCalpha to the CEMs, inducing PLD activation through the interaction of PKCalpha with PLD1 in the CEMs. Tetradecanoylphorbol Acetate protein kinase C, alpha Rattus norvegicus