Reversible phosphorylation of a protein from Trypanosoma equiperdum that exhibits homology with the regulatory subunits of mammalian cAMP-dependent protein kinases

Biochimie ◽  
2021 ◽  
Vol 181 ◽  
pp. 204-213
Author(s):  
José L. Escalona ◽  
José Bubis
Keyword(s):  
Protein Kinases ◽  
Reversible Phosphorylation ◽  
Regulatory Subunits ◽  
Dependent Protein ◽  
Trypanosoma Equiperdum

TSH action on cAMP binding to the regulatory subunits of cAMP-dependent protein kinases in pig thyroid cell cultures

1994 ◽  
Vol 99 (1) ◽  
pp. 103-110 ◽  
Author(s):  
M.Ben Abdelkhalek ◽  
M.F. Breton ◽  
D. Feliers ◽  
B. Haye ◽  
M. Pavlovic-Hournac
Keyword(s):  
Protein Kinases ◽  
Cell Cultures ◽  
Thyroid Cell ◽  
Regulatory Subunits ◽  
Dependent Protein

Retinoylation of the cAMP-binding regulatory subunits of type I and type II cAMP-dependent protein kinases in HL60 cells

1991 ◽  
Vol 290 (2) ◽  
pp. 293-302 ◽  
Author(s):  
Noriko Takahashi ◽  
Charis Liapi ◽  
Wayne B. Anderson ◽  
Theodore R. Breitman
Keyword(s):  
Protein Kinases ◽  
Type I ◽  
Type Ii ◽  
Regulatory Subunits ◽  
Hl60 Cells ◽  
Dependent Protein

scholarly journals Selective regulation of the amount of catalytic subunit of cyclic AMP-dependent protein kinases during isoprenaline-induced growth of the rat parotid gland

1987 ◽  
Vol 248 (1) ◽  
pp. 243-250 ◽  
Author(s):  
G Schwoch
Keyword(s):  
Cyclic Amp ◽  
Dna Synthesis ◽  
Protein Kinases ◽  
Catalytic Subunit ◽  
Regulatory Subunits ◽  
Rat Parotid Gland ◽  
C Subunit ◽  
Dependent Protein ◽  
Rat Parotid ◽  
Stimulation Of

Stimulation of growth of the rat parotid gland by repeated injection of the beta-agonist isoprenaline led to a significant decrease in the activity of cyclic AMP-dependent protein kinases. Immunochemical quantification of the catalytic (C) and regulatory (RI and RII) subunits of the cyclic AMP-dependent protein kinases type I and type II revealed a loss of 65% of the immunochemically measurable amount of catalytic subunit C. The amount of the regulatory subunits, however, remained constant. The observed decrease in C-subunit was not due to a translocation of the molecule to cellular membranes or to an inhibiting effect of the heat-stable inhibitor of cyclic AMP-dependent protein kinases. A selective decrease in only the C-subunit was also observed after a brief exposure to isoprenaline leading to the stimulation of DNA synthesis. Under these conditions, the decrease was observed at the onset of DNA synthesis (17 h after injection), but not at the the time of an earlier small cyclic AMP peak (13 h after injection) or at the time of maximal DNA synthesis (24 h after injection). The results indicate that the amount of the catalytic subunit of cyclic AMP-dependent protein kinases can be regulated independently from that of the regulatory subunits. The time-limited occurrence of the specific change in the amount of the C-subunit suggests that such a regulation is of physiological significance and that it may participate in cyclic AMP-mediated events involved in the control of cellular proliferation.

scholarly journals Evolution of the eukaryotic protein kinases as dynamic molecular switches

2012 ◽  
Vol 367 (1602) ◽  
pp. 2517-2528 ◽  
Author(s):  
Susan S. Taylor ◽  
Malik M. Keshwani ◽  
Jon M. Steichen ◽  
Alexandr P. Kornev
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Molecular Switches ◽  
Regulatory Subunits ◽  
Eukaryotic Protein ◽  
Activation Segment ◽  
Dynamic Assembly ◽  
Dependent Protein ◽  
Eukaryotic Protein Kinases

Protein kinases have evolved in eukaryotes to be highly dynamic molecular switches that regulate a plethora of biological processes. Two motifs, a dynamic activation segment and a GHI helical subdomain, distinguish the eukaryotic protein kinases (EPKs) from the more primitive eukaryotic-like kinases. The EPKs are themselves highly regulated, typically by phosphorylation, and this allows them to be rapidly turned on and off. The EPKs have a novel hydrophobic architecture that is typically regulated by the dynamic assembly of two hydrophobic spines that is usually mediated by the phosphorylation of an activation loop phosphate. Cyclic AMP-dependent protein kinase (protein kinase A (PKA)) is used as a prototype to exemplify these features of the PKA superfamily. Specificity in PKA signalling is achieved in large part by packaging the enzyme as inactive tetrameric holoenzymes with regulatory subunits that then are localized to macromolecular complexes in close proximity to dedicated substrates by targeting scaffold proteins. In this way, the cell creates discrete foci that most likely represent the physiological environment for cyclic AMP-mediated signalling.

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