AKAPs Bind PKA Regulatory Subunit Dimers
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چکیده
site for AKAPs the PKA an “hydrophobic Although a p dimers contai chains, the co generates a re difference in t posed as a me differentially i Highly loca by the uniqu associated wit AKAPs for RII variations wit late with diffe site (2, 111). F called Ht31, domain of AK to disrupt RII: much higher 1,030–1,277 n affinity betw AKAPs have a tion can be m analysis, and demonstrated affinities for s 1, a “dual AK (nM) affinity binds RII isof respectively) (46). AKAP95 entially bind threefold diffe vs. RII sugge in PKA ancho ences betwee represent an nism by whic highly localize
منابع مشابه
An entirely specific type I A-kinase anchoring protein that can sequester two molecules of protein kinase A at mitochondria.
A-kinase anchoring proteins (AKAPs) tether the cAMP-dependent protein kinase (PKA) to intracellular sites where they preferentially phosphorylate target substrates. Most AKAPs exhibit nanomolar affinity for the regulatory (RII) subunit of the type II PKA holoenzyme, whereas dual-specificity anchoring proteins also bind the type I (RI) regulatory subunit of PKA with 10-100-fold lower affinity. A...
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The subcellular localization of cAMP-dependent protein kinase (PKA) occurs through interaction with A-Kinase Anchoring Proteins (AKAPs). AKAPs bind to the PKA regulatory subunit dimer of both type Ialpha and type IIalpha (RIalpha and RIIalpha). RIalpha and RIIalpha display characteristic localization within different cell types, which is maintained by interaction of AKAPs with the N-terminal di...
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The cAMP protein kinase A (PKA) pathway in T cells conveys an inhibitory signal to suppress inflammation. This study was performed to understand the mechanisms involved in cAMP-mediated signaling in T lymphocytes. A-kinase anchoring proteins (AKAPs) bind and target PKA to various subcellular locations. AKAPs also bind other signaling molecules such as cyclic nucleotide phosphodiesterases (PDEs)...
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Subcellular compartmentalization of protein kinase A (PKA) by A-kinase anchoring proteins (AKAPs) facilitates local protein phosphorylation. However, little is known about how PKA targeting to AKAPs is regulated in the intact cell. PKA binds to an amphipathic helical region of AKAPs via an Nterminal domain of the regulatory subunit. In vitro studies showed that autophosphorylation of type II re...
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MOTIVATION Favorable interaction between the regulatory subunit of the cAMP-dependent protein kinase (PKA) and a peptide in A-kinase anchoring proteins (AKAPs) is critical for translocating PKA to the subcellular sites where the enzyme phosphorylates its substrates. It is very hard to identify AKAPs peptides binding to PKA due to the high sequence diversity of AKAPs. RESULTS We propose a hier...
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