A Common Phosphorylation Site for Cyclic AMP-dependent Protein Kinase and Protein Kinase C in Human Placental 6-Phosphofructo-2-kinase/Fructose-2,6-bisphosphatase

1998 ◽  
Vol 62 (10) ◽  
pp. 2039-2042 ◽  
Author(s):  
Noriko OKAMURA ◽  
Ryuzo SAKAKIBARA
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Phosphorylation Site ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Dependent Protein

scholarly journals Evidence for new phosphorylation sites for protein kinase C and cyclic AMP-dependent protein kinase in bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

FEBS Letters ◽  
1992 ◽  
Vol 310 (2) ◽  
pp. 139-142 ◽  
Author(s):  
Mark H. Rider ◽  
Josef Van Damme ◽  
Didier Vertommen ◽  
Alain Michel ◽  
Joël Vandekerckhove ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Phosphorylation Sites ◽  
Dependent Protein Kinase ◽  
Bovine Heart ◽  
Kinase C ◽  
Dependent Protein

scholarly journals Protein kinase C and cyclic AMP-dependent protein kinase phosphorylate phospholemman, an insulin and adrenaline-regulated membrane phosphoprotein, at specific sites in the carboxy terminal domain

1994 ◽  
Vol 304 (2) ◽  
pp. 635-640 ◽  
Author(s):  
S I Walaas ◽  
A J Czernik ◽  
O K Olstad ◽  
K Sletten ◽  
O Walaas
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Striated Muscle ◽  
Protein A ◽  
Phosphorylation Sites ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Kinase C ◽  
Dependent Protein

Phospholemman, a transmembrane, 72 residue protein enriched in striated muscle and heart [Palmer, Scott and Jones (1991) J. Biol. Chem. 266, 11126-11130], is phosphorylated in response to insulin [Walaas, Horn and Walaas (1991) Biochim. Biophys. Acta 1094, 92-102]. The present study is aimed at identifying the phosphorylation sites of this protein. A synthetic peptide, GTFRSS63IRRLS68TRRR (in the single letter code) and consisting of phospholemman residues 58-72, is a substrate for both protein kinase C and cyclic AMP (cAMP)-dependent protein kinase, with Km values of 6-7 microM for both enzymes. Amino acid sequencing of the phosphopeptide shows that protein kinase C phosphorylates both Ser-63 and Ser-68, while cAMP-dependent protein kinase phosphorylates Ser-68. Thermolytic phosphopeptide mapping of 32P-labelled phospholemman from rat diaphragms shows that treatment with insulin results in labelling of phosphopeptides containing both Ser-63 and Ser-68, whereas treatment with adrenaline results in labelling of the phosphopeptide containing Ser-68. Hence, insulin and adrenaline regulate the phosphorylation of phospholemman, presumably through protein kinase C and cAMP-dependent protein kinase, respectively, on partly overlapping phosphorylation sites.

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