Title : Phosphorylation and activation of phospholipase D1 by protein kinase C in vivo: determination of multiple phosphorylation sites.

Pub. Date : 1999 Aug 10

PMID : 10441128






8 Functional Relationships(s)
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1 For the first time, we have now identified multiple basal phophopeptides and multiple phorbol myristate acetate (PMA) induced phosphopeptides of endogenous PLD1 in 3Y1 cells as well as of transiently expressed PLD1 in COS-7 cells. Tetradecanoylphorbol Acetate phospholipase D1 Rattus norvegicus
2 For the first time, we have now identified multiple basal phophopeptides and multiple phorbol myristate acetate (PMA) induced phosphopeptides of endogenous PLD1 in 3Y1 cells as well as of transiently expressed PLD1 in COS-7 cells. Tetradecanoylphorbol Acetate phospholipase D1 Rattus norvegicus
3 For the first time, we have now identified multiple basal phophopeptides and multiple phorbol myristate acetate (PMA) induced phosphopeptides of endogenous PLD1 in 3Y1 cells as well as of transiently expressed PLD1 in COS-7 cells. Tetradecanoylphorbol Acetate phospholipase D1 Rattus norvegicus
4 Interestingly, threonine 147 is located in the PX domain and serine 561 is in the negative regulatory "loop" region of PLD1. Threonine phospholipase D1 Rattus norvegicus
5 Interestingly, threonine 147 is located in the PX domain and serine 561 is in the negative regulatory "loop" region of PLD1. Serine phospholipase D1 Rattus norvegicus
6 Mutation of serine 2, threonine 147, or serine 561 significantly reduced PMA-induced PLD1 activity. Serine phospholipase D1 Rattus norvegicus
7 Mutation of serine 2, threonine 147, or serine 561 significantly reduced PMA-induced PLD1 activity. Threonine phospholipase D1 Rattus norvegicus
8 Mutation of serine 2, threonine 147, or serine 561 significantly reduced PMA-induced PLD1 activity. Serine phospholipase D1 Rattus norvegicus