Cross Talk between Protein Kinase A and Androgen Signaling Pathway

2015 ◽  
Vol 19 (1) ◽  
pp. 1 ◽  
Author(s):  
Manisha Dagar ◽  
Gargi Bagchi Bhattacharjee
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Signaling Pathway ◽  
Cross Talk ◽  
Kinase A

scholarly journals Protein Kinase A Signaling Pathway Regulates Transcriptional Activity of SAF-1 by Unmasking Its DNA-binding Domains

2003 ◽  
Vol 278 (25) ◽  
pp. 22586-22595 ◽  
Author(s):  
Alpana Ray ◽  
Papiya Ray ◽  
Nicole Guthrie ◽  
Arvind Shakya ◽  
Deepak Kumar ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dna Binding ◽  
Protein Kinase A ◽  
Signaling Pathway ◽  
Transcriptional Activity ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Kinase A

scholarly journals Two PKA RIα holoenzyme states define ATP as an isoform-specific orthosteric inhibitor that competes with the allosteric activator, cAMP

2019 ◽  
Vol 116 (33) ◽  
pp. 16347-16356 ◽  
Author(s):  
Tsan-Wen Lu ◽  
Jian Wu ◽  
Phillip C. Aoto ◽  
Jui-Hung Weng ◽  
Lalima G. Ahuja ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Cross Talk ◽  
Structural Diversity ◽  
Dimer Interface ◽  
Biochemical Studies ◽  
Allosteric Mechanisms ◽  
Allosteric Activator ◽  
Kinase A ◽  
In Cells

Protein kinase A (PKA) holoenzyme, comprised of a cAMP-binding regulatory (R)-subunit dimer and 2 catalytic (C)-subunits, is the master switch for cAMP-mediated signaling. Of the 4 R-subunits (RIα, RIβ, RIIα, RIIβ), RIα is most essential for regulating PKA activity in cells. Our 2 RIα2C2 holoenzyme states, which show different conformations with and without ATP, reveal how ATP/Mg2+ functions as a negative orthosteric modulator. Biochemical studies demonstrate how the removal of ATP primes the holoenzyme for cAMP-mediated activation. The opposing competition between ATP/cAMP is unique to RIα. In RIIβ, ATP serves as a substrate and facilitates cAMP-activation. The isoform-specific RI-holoenzyme dimer interface mediated by N3A–N3A′ motifs defines multidomain cross-talk and an allosteric network that creates competing roles for ATP and cAMP. Comparisons to the RIIβ holoenzyme demonstrate isoform-specific holoenzyme interfaces and highlights distinct allosteric mechanisms for activation in addition to the structural diversity of the isoforms.

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