Title : Overexpression of myristoylated alanine-rich C-kinase substrate enhances activation of phospholipase D by protein kinase C in SK-N-MC human neuroblastoma cells.

Pub. Date : 1998 Jun 1

PMID : 9601059






3 Functional Relationships(s)
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1 Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient. Phosphatidylcholines myristoylated alanine rich protein kinase C substrate Homo sapiens
2 Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient. Phosphatidylcholines myristoylated alanine rich protein kinase C substrate Homo sapiens
3 Our results show that MARCKS is an essential link in the PKC-mediated activation of PtdCho-specific PLD in these cells and that the stimulation of PtdCho synthesis by PMA is a secondary response. Phosphatidylcholines myristoylated alanine rich protein kinase C substrate Homo sapiens