The expression of 80K/MARCKS, a major substrate of protein kinase C (PKC), is down-regulated through both PKC-dependent and -independent pathways. Effects of bombesin, platelet-derived growth factor, and cAMP.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference64 articles.
1. Studies and Perspectives of Protein Kinase C
2. Early Signals Underlying the induction of the c-fos and c-myc Genes in Quiescent Fibroblasts: Studies with Bombesin and Other Growth Factors
3. Phorbol esters, phospholipase C, and growth factors rapidly stimulate the phosphorylation of a Mr 80,000 protein in intact quiescent 3T3 cells.
4. c-myc gene expression is stimulated by agents that activate protein kinase C and does not account for the mitogenic effect of PDGF
5. Serum, like phorbol esters, rapidly activates protein kinase C in intact quiescent fibroblasts.
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3. Protein Kinase D Mediates Mitogenic Signaling by Gq-coupled Receptors through Protein Kinase C-independent Regulation of Activation Loop Ser744 and Ser748 Phosphorylation;Journal of Biological Chemistry;2009-05
4. MARCKS is a downstream effector in platelet-derived growth factor-induced cell motility in activated human hepatic stellate cells;Experimental Cell Research;2008-04
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