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Data show that laminin alpha2beta1gamma1 (Lm211) can inhibit neuregulin 1 (show NRG1 ELISA Kits) type III (Nrg1III) by limiting protein kinase A (PKA) activation, which is required to initiate myelination.
study identifies a new role of Dual-AKAP1 in regulating mitochondrial trafficking through Miro-2, and supports a model in which PINK1 and mitochondrial PKA participate in a similar neuroprotective signaling pathway to maintain dendrite connectivity
Data suggest that enzyme activation by cAMP involves highly stable conformation of Prkar1a as it binds to Prkaca; glycine residue, G235, appears to function as hinge in B/C helix conserved in Prkar1a; this "Flipback" conformation plays role in cAMP association to A domain of Prkar1a. (Prkar1a = cyclic AMP-dependent protein kinase RIalpha subunit; Prkaca = cyclic AMP-dependent protein kinase catalytic subunit)
cAMP dependent protein kinase A (PKA) is a key intracellular factor mediating SHH (show SHH ELISA Kits) signaling through regulation of GLI3 (show GLI3 ELISA Kits) processing.
this study shows illustrates for the first time the ability of protein kinase A to increase colony-stimulating factor 1 receptor (show CSF1R ELISA Kits) DNA methylation (show HELLS ELISA Kits) resulting in macrophage maturation
these results suggest that the activation of 5-HT1D receptors selectively enhanced IA via the Gbetagamma of the Go-protein, PKA, and the sequential B-Raf (show SNRPE ELISA Kits)-dependent p38 MAPK (show MAPK14 ELISA Kits) signaling cascade.
These data indicate that LPA increases CCN2 (show CTGF ELISA Kits) expression through the activation of PKC (show PKC ELISA Kits) and PKA. Thus, the regulatory functions of the PKC (show PKC ELISA Kits) and PKA pathways are implicated in the LPA-induced increase in CCN2 (show CTGF ELISA Kits) expression
PKA phosphorylates the ATPase inhibitory factor 1 (show ATPIF1 ELISA Kits) and inactivates its capacity to bind and inhibit the mitochondrial H(+)-ATP synthase.
Data suggest PRKAR1A (show PRKAR1A ELISA Kits) contains two structurally homologous cAMP-binding domains that exhibit marked differences in dynamic profiles in activation/inhibition of Prkaca; conservation of structure does not necessarily imply conservation of dynamics.
Data (including data from studies in transgenic mice) suggest that constitutive activation of Prkaca in osteoblasts is sufficient to increase bone mass, favorably modify bone architecture, and improve mechanical properties of bone.
The mutated PRKACA proteins lost their ability to bind to PRKAR1A (show PRKAR1A ELISA Kits), and thereby lead to constitutive activation of the PKA pathway. Together with previous reports of PRKAR1A (show PRKAR1A ELISA Kits) mutations in syndromic cardiac myxoma, our study demonstrates the importance of the PKA pathway in the tumourigenesis of cardiac myxoma.
differential regulation of PKA and cell stiffness in unconfined versus confined cells is abrogated by dual, but not individual, inhibition of Piezo1 and myosin II.
PRKACA mutations are present in cortisol-producing adenomas and bilateral adrenal macronodular hyperplasia. PRKACA mutation is associated with more severe autonomous cortisol secretion.
Dual co-expression of human fetal Tau with PKA in Escherichia coli results in multisite Tau phosphorylation including also naturally occurring sites which were not previously considered in the context of 14-3-3 (show YWHAQ ELISA Kits) binding. Tau protein co-expressed with PKA displays tight functional interaction with 14-3-3 (show YWHAQ ELISA Kits) isoforms of a different type.
This review will discuss the effects of PKA phosphorylation on wild-type CFTR (show CFTR ELISA Kits), the consequences of cystic fibrosis (show S100A8 ELISA Kits) mutations on PKA phosphorylation, and the development of therapies that target PKA-mediated signaling. [review]
This interaction is promoted by EPAC1 (show RAPGEF3 ELISA Kits) activation, triggering its translocation to the plasma membrane and binding to NHERF1 (show SLC9A3R1 ELISA Kits). Our findings identify a new CFTR (show CFTR ELISA Kits)-interacting protein and demonstrate that cAMP activates CFTR (show CFTR ELISA Kits) through two different but complementary pathways - the well-known PKA-dependent channel gating pathway and a new mechanism regulating endocytosis that involves EPAC1 (show RAPGEF3 ELISA Kits).
The inhibitory effects of BMP4 (show BMP4 ELISA Kits) on PDGF (show PDGFA ELISA Kits)-induced cell proliferation, collagen synthesis, and calpain-2 (show CAPN2 ELISA Kits) activation are impaired in pulmonary artery smooth muscle cells from pulmonary arterial hypertension patient.
description of PRKACA mutations in 2 cases of primary aldosteronism (PA) patients: a novel variant (p.His88Asp) in a case of sudden onset of PA and a mutation (p.Leu206Arg) in context of hypokalemic aggravation of long-term hypertension; these genetic alterations were not found in a subsequent series of 120 aldosterone-producing adenomas and thereby appear to be very rare events
PKA signaling is pivotal in pigmentation process itself in cultured melanoma cells, while the importance of Wnt (show WNT2 ELISA Kits)/beta-catenin (show CTNNB1 ELISA Kits) signaling should be emphasized in the context of development and differentiation
Studies indicate a functional interaction between leucine-rich repeat kinase 2 (LRRK2 (show LRRK2 ELISA Kits)) and protein kinase A (PKA) cross-talk in neuron and microglia.
ceramide as a potent physiological modulator of the Na(+)-ATPase (show DNAH8 ELISA Kits), participating in a regulatory network in kidney cells and counteracting the stimulatory effect of PKA via PKCzeta (show PRKCZ ELISA Kits)
we demonstrate that PKA, PKC (show FYN ELISA Kits) and PI3K pathways crosstalk in porcine male germ cells to crucially regulate GSK3A (show GSK3a ELISA Kits) phosphorylation which subsequently controls cell motility.
PKA and MEK (thus, also pERK) are the intracellular mediators downstream of GPR30 that induce the non-genomic suppression of GnRH-induced LH secretion from bovine AP cells by estradiol or G1
Data indicate that mitochondrial cAMP-dependent protein kinase (PKA) activity is regulated by the protease calpain.
structural basis of selectivity for protein kinase A in complex with Rho-kinase (show ROCK1 ELISA Kits) inhibitors by x-ray crystallography
Purification and characterisation of protein kinase catalytic subunit (PKAcat) from bovine lens.
Cyclic AMP-dependent protein kinase A (PKA) is an essential enzyme in the signaling pathway of the second messenger cAMP. Through phosphorylation of target proteins, PKA controls many biochemical events in the cell including regulation of metabolism, ion transport, and gene transcription. The PKA holoenzyme is composed of 2 regulatory and 2 catalytic subunits and dissociates from the regulatory subunits upon binding of cAMP.
, cAMP-dependent protein kinase catalytic subunit alpha
, sperm cAMP-dependent protein kinase catalytic subunit
, protein kinase A catalytic subunit
, protein kinase, cAMP-dependent, catalytic, alpha
, C-alpha subunit
, protein kinase A
, cAMP-dependent protein kinase catalytic subunit C alpha
, protein kinase A alpha
, cAMP-dependent protein kinase type I-beta regulatory subunit