The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins.

1987 ◽  
Vol 6 (6) ◽  
pp. 1599-1604 ◽  
Author(s):  
K. Weber ◽  
N. Johnsson ◽  
U. Plessmann ◽  
P. N. Van ◽  
H. D. Söling ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Domain Structure ◽  
Binding Proteins ◽  
Phosphorylation Site ◽  
Lipid Binding ◽  
Kinase C ◽  
Lipid Binding Proteins

scholarly journals Amino acid sequence and characterization of a protein inhibitor of protein kinase C.

1990 ◽  
Vol 265 (8) ◽  
pp. 4583-4591 ◽  
Author(s):  
J D Pearson ◽  
D B DeWald ◽  
W R Mathews ◽  
N M Mozier ◽  
H A Zürcher-Neely ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Protein Inhibitor ◽  
Kinase C

scholarly journals Influence of lipid on the structure and phosphorylation of protein kinase C α substrate peptides

1998 ◽  
Vol 330 (3) ◽  
pp. 1433-1442 ◽  
Author(s):  
B. Betsy VINTON ◽  
L. Stacey WERTZ ◽  
Jaison JACOB ◽  
Joanna STEERE ◽  
M. Charles GRISHAM ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Structural Change ◽  
Protein Kinase ◽  
Phosphorylation Site ◽  
Cd Spectroscopy ◽  
Lipid Binding ◽  
Bovine Brain ◽  
Helical Conformation ◽  
Spin Labels ◽  
Kinase C

The structure and phosphorylation of two protein kinase C (PKC) α substrate peptides were investigated in varying lipid systems using enzyme activity assays and circular dichroism (CD) spectroscopy. The α-peptide, which exhibits the typical PKC α substrate motif and is based on the pseudosubstrate region of PKC α, was phosphorylated to a similar extent in bovine brain phosphatidylserine vesicles or diheptanoylphosphatidylcholine (PC7) micelles (both with 5 mol % 1,2-dioleoyl-sn-glycerol), whereas neuromodulin (NM)-peptide, which does not exhibit this motif by virtue of its primary structure, was phosphorylated to a much lesser extent in the PC7 micellar system. CD spectra of the peptides indicated that NM-peptide underwent a dramatic structural change in the presence of dimyristoylphosphatidylserine (DMPS) vesicles, whereas spectra acquired in PC7 micelles were similar to those acquired in buffer alone. No significant structural change was observed in the α-peptide in the presence of either lipid. PKC activity assays conducted with a series of NM-peptides successively substituted with nitroxide spin labels at each residue position suggested that several residues distal to the phosphorylation site are necessary for substrate recognition. The effect of these substitutions is not consistent with the binding of the NM-peptide to PKC in an extended structure, but is consistent with the binding of this peptide in a helical conformation. Furthermore, the docking of a helical NM-peptide to the substrate binding site of PKC suggests that the interaction is energetically feasible. These results suggest that PKC may recognize some non-linear substrate motifs and that lipid binding may convert a protein into a better PKC substrate.

scholarly journals Amino acid sequence of a 12-kDa inhibitor of protein kinase C

1990 ◽  
Vol 194 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Ned M. MOZIER ◽  
Heidi A. ZURCHER-NEELY ◽  
David M. GUIDO ◽  
W. Rodney MATHEWS ◽  
Robert L. HEINRIKSON ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Kinase C

scholarly journals Different pathways for control of Na+/H+ exchange via activation of the thrombin receptor

1994 ◽  
Vol 297 (1) ◽  
pp. 47-52 ◽  
Author(s):  
R Nieuwland ◽  
G van Willigen ◽  
J W N Akkerman
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Sequence ◽  
Rapid Decrease ◽  
Thrombin Receptor ◽  
Cytosolic Ph ◽  
Kinase C ◽  
Different Types ◽  
Sustained Increase

The aim of the present study was to clarify the control of Na+/H+ exchange in platelets activated via the thrombin receptor. When human BCECF-loaded platelets were stimulated with the thrombin-receptor-activating peptide (TRAP; amino acid sequence SFLLRN), which activates the receptor independently of proteolysis, the cytosolic pH (pHi) rose from 7.13 +/- 0.04 (n = 6) to 7.27 +/- 0.04 (n = 5), followed by a rapid decrease to resting values. Trypsin, which cleaves the receptor, induced a rapid and irreversible rise in pHi to 7.31 +/- 0.06 (n = 5). gamma-Thrombin, which cleaves the receptor but is unable to bind to the hirudin-like domain, induced a slow and irreversible rise in pHi to 7.31 +/- 0.04 (n = 14). alpha-Thrombin, which cleaves the receptor and binds to its hirudin-like domain, induced a rapid and irreversible rise in pHi to 7.31 +/- 0.04 (n = 22). Changes in pHi induced by TRAP, trypsin, gamma- and alpha-thrombin were accompanied by similar changes in cytosolic Ca2+ concentration ([Ca2+]i) and 32P-pleckstrin, a substrate of protein kinase C (PKC). The separate chelation of Ca2+i (30 microM BAPTA-AM) or inhibition of PKC (1 microM staurosporine) induced about 50% inhibition of the pHi responses triggered by TRAP, trypsin, gamma- and alpha-thrombin, but the combination induced complete inhibition. Thus the different types of activation of the thrombin receptor control Na+/H+ exchange via the same mechanism. Binding of thrombin to the hirudin-like domain accelerates exchange activation, whereas proteolysis of the receptor is essential for a sustained increase in pHi.

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