EC Number   |
General Information |
Reference |
|---|
   2.7.11.11 | evolution |
cAMP-dependent protein kinases are a major regulator of signal transduction that arose prior to the origin of multicellularity in eukaryotes. In mammalian protein kinase A (PKAs), the two binding sites of the regulatpory R subunits display positive cooperativity upon cAMP binding. The C-terminal CBD2, or B site, is always exposed and immediately available for nucleotide binding. When this site is occupied, it stabilizes structural changes within CBD1 that drastically increase its affinity for cAMP and promote subunit dissociation and hence activation. The regulatory subunit of Plasmodium falciparum protein kinase A (PfPKA-R) utilizes a similar two-state cooperative binding mechanism that provides an enthalpically driven interaction with nanomolar affinity for cAMP, as in vertebrates |
761455 |
| 2.7.11.11 | evolution |
exploration and elucidation of the evolution of the alternative 5' exons and the splicing pattern giving rise to the numerous PKA catalytic subunit isoforms. Alignment of the segments encoded by Calpha1- and Cbeta1-specific 5'exons |
762227 |
| 2.7.11.11 | malfunction |
catalytic subunit of cAMP-dependent protein kinase A silencing results in reduced conidiation and conidium morphogenesis |
722298 |
| 2.7.11.11 | malfunction |
combined inhibition of the androgen receptor and the regulatory subunit I alpha of PKA with small interference RNAs significantly increases the growth-inhibitory and proapoptotic effects of androgen receptor knockdown. Downregulating PKA RIalpha is sufficient to inhibit PKA signaling and also impairs androgen receptor expression and activation. Depletion of PKA RIalpha also potentiates the antiproliferative effect of the antiandrogen bicalutamide in androgen-sensitive LNCaP cells |
708764 |
| 2.7.11.11 | malfunction |
downregulation of gene pfpkac mRNA using gene silencing leads to morphological changes in schizont stages and cell cycle arrest, and is also associated with a compensatory decrease in pfpkar mRNA levels, suggesting a transcriptional self-regulation of the PfPKA signalling network |
723339 |
| 2.7.11.11 | malfunction |
enzyme inhibition leads to hypersprouting as a result of an increased number of tip cells |
738093 |
| 2.7.11.11 | malfunction |
enzyme-deficient cells show a higher glutathione reductase expression level and are less sensitive to cell killing and generation of malondialdehyde than are wild-type cells incubated with H2O2 |
721681 |
| 2.7.11.11 | malfunction |
inhibition of PKA reduces accuracy in the 5-choice serial reaction time task and causes substantial increases in locomotor activity without affecting motivation or the capacity to emit operant responses at high rates, PKA inhibition within the medial prefrontal cortex of rats produces inattention and hyperactivity |
710100 |
| 2.7.11.11 | malfunction |
inhibition of PKA with KT5720 abolishes lactic-acid- or contraction-induced ATP release from muscle |
-, 723596 |
| 2.7.11.11 | malfunction |
protein kinase A Calpha and Cbeta ablation both results in a 50% reduction in PKA-specific kinase activity and the level of PKA type I but not PKA type II, PKA subunit Calpha but not Cbeta ablation augments expression of the activation marker CD69 on lymphocytes |
703141 |
