Binding of Myristoylated Alanine-Rich Protein Kinase C Substrate to Phosphoinositides Attenuates the Phosphorylation by Protein Kinase C

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Arch Biochem Biophys | / 2卷 / 193期

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[1] Binding of myristoylated alanine-rich protein kinase C substrate to phosphoinositides attenuates the phosphorylation by protein kinase C
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[2] Importance of protein kinase C targeting for the phosphorylation of its substrate, myristoylated alanine-rich C-kinase substrate
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[3] CHARACTERIZATION OF THE PHOSPHORYLATION SITES IN THE CHICKEN AND BOVINE MYRISTOYLATED ALANINE-RICH C-KINASE SUBSTRATE PROTEIN, A PROMINENT CELLULAR SUBSTRATE FOR PROTEIN KINASE-C
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[8] Neurotensin release in response to protein kinase C activation by phorbol esters is mediated through myristoylated alanine-rich C kinase substrate phosphorylation
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[9] Protein kinase C-mediated phosphorylation of the myristoylated alanine-rich C-kinase substrate protects it from specific proteolytic cleavage
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[10] Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes
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