Cyclic nucleotide dependent protein kinase and the phosphorylation of endogenous proteins of retinal rod outer segments

Biochemistry ◽  
1979 ◽  
Vol 18 (2) ◽  
pp. 370-378 ◽  
Author(s):  
Debora B. Farber ◽  
Bruce M. Brown ◽  
Richard N. Lolley
Keyword(s):  
Protein Kinase ◽  
Cyclic Nucleotide ◽  
Rod Outer Segments ◽  
Dependent Protein Kinase ◽  
Outer Segments ◽  
Retinal Rod ◽  
Dependent Protein ◽  
Endogenous Proteins ◽  
Retinal Rod Outer Segments

scholarly journals Regulation by light of cyclic nucleotide-dependent protein kinases and their substrates in frog rod outer segments.

1990 ◽  
Vol 95 (3) ◽  
pp. 545-567 ◽  
Author(s):  
H Hamm
Keyword(s):  
Protein Kinase ◽  
Cyclic Nucleotide ◽  
Soluble Fraction ◽  
Subcellular Fractionation ◽  
Rod Outer Segments ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Outer Segments ◽  
Dependent Protein ◽  
Membrane Bound

Cyclic nucleotides (both cAMP and cGMP) stimulate the phosphorylation of several proteins of 65-70, 50-52, 21, 13, and 12 kD in rod outer segments (ROS) of the frog retina. Subcellular fractionation showed that phosphopeptides of 67, 21, 13, and 12 kD were soluble and phosphopeptides of 69, 67, 50-52, and 12 kD were membrane associated at physiological ionic strength. Components I and II, 13 and 12 kD, respectively, are the major cyclic nucleotide-dependent phosphoproteins of ROS and have been reported to be phosphorylated in the dark and dephosphorylated in the light. Under unstimulated conditions, phosphorylated Components I and II were found in the soluble fraction. Cyclic nucleotide stimulation of phosphorylation resulted in increased phospho-Components I and II in the soluble fraction, and phospho-Component II on the membrane. Light had no effect on the phosphorylation level of soluble Components I and II, but it caused a depletion within 1 s of the membrane-bound phospho-Component II. A half-maximal decrease in membrane-bound Component II was seen at 5 x 10(5) rhodopsins bleached per outer segment. The cyclic nucleotide-dependent protein kinase(s) were found primarily in the peripheral membrane fraction of ROS proteins. 8-bromo cyclic AMP was two orders of magnitude more effective than 8-bromo cyclic GMP at stimulating Component I and II phosphorylation. An active peptide of the Walsh inhibitor of cAMP-dependent protein kinase [PKI(5-22)amide] blocked the phosphorylation with an IC50 of 10 nM. Photoaffinity labeling studies with 8-N3-cAMP and 8-N3-cGMP revealed the presence of a 52-kD band specifically labeled with 8-N3-cAMP, but no specific 8-N3-cGMP labeling. These data suggest that cyclic nucleotide-dependent protein phosphorylation in ROS occurs via the activation of a cAMP-dependent protein kinase.

scholarly journals Structural basis of cyclic nucleotide selectivity in cGMP dependent protein kinase II

2015 ◽  
Vol 16 (S1) ◽  
Author(s):  
James C. Campbell ◽  
Kevin Y. Li ◽  
Jeong Joo Kim ◽  
Gilbert Huang ◽  
Albert S. Reger ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclic Nucleotide ◽  
Structural Basis ◽  
Dependent Protein Kinase ◽  
Cgmp Dependent Protein Kinase ◽  
Protein Kinase Ii ◽  
Dependent Protein

scholarly journals Mg2+ -ATP induces filament growth from retinal rod outer segments with disrupted plasma membranes

FEBS Letters ◽  
1987 ◽  
Vol 211 (1) ◽  
pp. 35-40 ◽  
Author(s):  
K.R. Parker ◽  
L.E. Schaechter ◽  
J.W. Lewis ◽  
K.L. Zeman ◽  
D.S. Kliger ◽  
...  
Keyword(s):  
Plasma Membranes ◽  
Rod Outer Segments ◽  
Outer Segments ◽  
Retinal Rod ◽  
Retinal Rod Outer Segments
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