scholarly journals Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity.

1986 ◽  
Vol 261 (18) ◽  
pp. 8140-8145 ◽  
Author(s):  
D K Blumenthal ◽  
K Takio ◽  
R S Hansen ◽  
E G Krebs
Keyword(s):  
Protein Kinase ◽  
Substrate Specificity ◽  
Protein Phosphatase ◽  
Regulatory Subunit ◽  
Type Ii ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals Properties of the regulatory subunit of cAMP-dependent protein kinase type II from human brain

IUBMB Life ◽  
1996 ◽  
Vol 40 (6) ◽  
pp. 1159-1166
Author(s):  
I. D. Grozdova ◽  
N. A. Alexandrova ◽  
E. V. Sveshnikova ◽  
N. S. Melik-Nubarov ◽  
P. G. Sveshnikov ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Human Brain ◽  
Regulatory Subunit ◽  
Type Ii ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

scholarly journals Immunogold localization of the regulatory subunit of a type II cAMP-dependent protein kinase tightly associated with mammalian sperm flagella.

1988 ◽  
Vol 107 (5) ◽  
pp. 1809-1816 ◽  
Author(s):  
S J Lieberman ◽  
W Wasco ◽  
J MacLeod ◽  
P Satir ◽  
G A Orr
Keyword(s):  
Monoclonal Antibody ◽  
Protein Kinase ◽  
Mitochondrial Membrane ◽  
Regulatory Subunit ◽  
Type Ii ◽  
Outer Mitochondrial Membrane ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Mammalian Sperm ◽  
Dependent Protein

We have shown previously that the regulatory subunit (RII) of a type II cAMP-dependent protein kinase is an integral component of the mammalian sperm flagellum (Horowitz, J.A., H. Toeg, and G.A. Orr. 1984. J. Biol. Chem. 259:832-838; Horowitz, J.A., W. Wasco, M. Leiser, and G.A. Orr. 1988. J. Biol. Chem. 263:2098-2104). The subcellular localization of this flagellum-associated RII in bovine caudal epididymal sperm was analyzed at electron microscope resolution with gold-conjugated secondary antibody labeling techniques using anti-RII monoclonal antibodies. By immunoblot analysis, the flagellum-associated RII was shown to interact with mAb 622 which cross reacts with both neural and nonneural isoforms of RII. In contrast, a neural specific monoclonal antibody (mAb 526) failed to interact with flagellar RII. In the midpiece of the demembranated sperm tail, gold label after mAb 622 incubation was primarily associated with the outer mitochondrial membrane. Although almost all specific labeling in the midpiece can be assigned to the mitochondria, in the principal piece, there is some labeling of the fibrous sheath. Labeling of the outer dense fibers and the axoneme was sparse. Specific labeling was virtually absent in the sperm head. Sections of sperm tails incubated in the absence of primary antisera or with mAb 526 showed little labeling. A beta-tubulin monoclonal antibody localized only to the 9 + 2 axoneme. These results raise the possibility that a type II cAMP-dependent protein kinase located at the outer mitochondrial membrane plays a role in the direct cAMP stimulation of mitochondrial respiration during sperm activation.

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