Solution structure of the cAMP-dependent protein kinase catalytic subunit and its contraction upon binding the protein kinase inhibitor peptide

Biochemistry ◽  
1993 ◽  
Vol 32 (14) ◽  
pp. 3649-3657 ◽  
Author(s):  
G. A. Olah ◽  
R. D. Mitchell ◽  
T. R. Sosnick ◽  
D. A. Walsh ◽  
J. Trewhella
Keyword(s):  
Protein Kinase ◽  
Solution Structure ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Catalytic Subunit ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Inhibitor Peptide ◽  
Dependent Protein

The protein kinase A catalytic subunit Cβ2: molecular characterization and distribution of the splice variant

2000 ◽  
Vol 351 (1) ◽  
pp. 123-132 ◽  
Author(s):  
Sandra THULLNER ◽  
Frank GESELLCHEN ◽  
Stefan WIEMANN ◽  
Walter PYERIN ◽  
Volker KINZEL ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Splice Variant ◽  
Cardiac Tissue ◽  
Kinase Inhibitor ◽  
Morphological Changes ◽  
Affinity Purification ◽  
Catalytic Subunit ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein

Cβ2, a 46 kDa splice variant of the Cβ isoform, is the largest isoform so far described for catalytic subunits from cAMP-dependent protein kinase in mammals. It differs from Cβ in the first 15 N-terminal residues which are replaced with a 62-residue domain with no similarity to other known proteins. The Cβ2 protein was identified in cardiac tissue by MS, microsequencing and C-subunit-isoform-selective antibodies. The Cβ2 protein has a very low abundance of about 2% of total affinity-purified C subunits from bovine cardiac tissue. This, and the similarity of its biochemical properties to Cα and Cβ, are probably some of the reasons why the Cβ2 protein has escaped detection so far. The abundance of the Cβ2 protein differs dramatically between tissues, with most protein detected in heart, liver and spleen, and the lowest level in testis. Cβ2 protein shows kinase activity against synthetic substrates, and is inhibited by the protein kinase inhibitor peptide PKI(5-24). The degree of Cβ2 removal from tissue extracts by binding to PKI(5-24) depends on the cAMP level, i.e. on the dissociation state of the holoenzyme. Two sites in the protein are phosphorylated: Thr-244 in the activation segment and Ser-385 close to the C-terminus. By affinity purification and immunodetection Cβ2 was found in cattle, pig, rat, mouse and turkey tissue and in HeLa cells. In the cAMP-insensitive CHO 10260 cell line, which has normal Cβ but is depleted of Cα, stable transfection with Cβ2 restored most of the cAMP-induced morphological changes. Cβ2 is a ubiquitously expressed protein with characteristic properties of a cAMP-dependent protein kinase catalytic subunit.

scholarly journals The H89 cAMP-dependent protein kinase inhibitor blocks Plasmodium falciparum development in infected erythrocytes

2001 ◽  
Vol 268 (18) ◽  
pp. 4842-4849 ◽  
Author(s):  
Chiang Syin ◽  
Daniel Parzy ◽  
Francois Traincard ◽  
Irène Boccaccio ◽  
Manju B. Joshi ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Protein Kinase ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein
Sign in / Sign up

Export Citation Format

Share Document