Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein

Wang, Lin; Sunahara, Roger K.; Krumins, Andrejs M.; Perkins, Guy; Crochiere, Marsha; Mackey, Mason; Bell, Sean; Ellisman, Mark H.; Taylor, Susan S.

doi:10.1073/pnas.051633398

Cited by 93 publications

(81 citation statements)

References 49 publications

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“…Most analyses of PKA anchoring have focused on AKAPs that interact with RII, especially RII␣ (9,18). So-called dual AKAPs, such as D-AKAP1 and D-AKAP2, can interact with both RI and RII (14,15), and there are several AKAPs that associate specifically with RI or RI-like subunits, such as AKAP CE (19,20). RI␤ has been implicated in the presynaptic regulation of hippocampal LTP͞LTD and in vivo with synaptic plasticity in the visual cortex (21-23), but no AKAP for RI␤ was identified in those systems.…”

Section: Discussionmentioning

confidence: 99%

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Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)

Adamik

Pacheco–Rodriguez

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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Like other guanine nucleotide-exchange proteins (GEPs) that activate ADP-ribosylation factor (ARF) GTPases, brefeldin A-inhibited GEP2, BIG2, contains an Ϸ200-aa Sec7 domain that is responsible for this catalytic activity and its inhibition by brefeldin A. The Sec7 domain is located near the center of the molecule and serves to accelerate replacement of GDP bound to ARF with GTP. To explore possible functions of the N-terminal region of BIG2 (1-832), we used three coding-region constructs as bait to screen a human heart cDNA library in a yeast two-hybrid system, retrieving two unique clones that encode a type I protein kinase

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Section: Discussionmentioning

confidence: 99%

“…Classical AKAPs that anchor type II PKA holoenzymes, contain an amphipathic helix of 14-18 amino acids that binds the N termini of homodimers of RII␣ or RII␤ (12,13). So-called dual AKAPs interact with both RI and RII subunits (14,15).…”

mentioning

confidence: 99%

Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)

Adamik

Pacheco–Rodriguez

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

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“…D-AKAP2, dual specificity A kinase anchoring protein 2, binds the regulatory subunit of cAMP-dependent protein kinase and has 2 RH domains. However, no G protein interaction has been reported for this protein (33).…”

mentioning

confidence: 99%

G Protein-coupled Receptor Kinase 2/Gαq/11 Interaction

Sterne‐Marr

Tesmer

Day

et al. 2003

Journal of Biological Chemistry

113

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G protein-coupled receptors (GPCRs) transduce cellular signals from hormones, neurotransmitters, light, and odorants by activating heterotrimeric guanine nucleotide-binding (G) proteins. For many GPCRs, short term regulation is initiated by agonist-dependent phosphorylation by GPCR kinases (GRKs), such as GRK2, resulting in G protein/receptor uncoupling. GRK2 also regulates signaling by binding G␣ q/ll and inhibiting G␣ q stimulation of the effector phospholipase C␤. The binding site for G␣ q/ll resides within the amino-terminal domain of GRK2, which is homologous to the regulator of G protein signaling (RGS) family of proteins. To map the G␣ q/ll binding site on GRK2, we carried out site-directed mutagenesis of the RGS homology (RH) domain and identified eight residues, which when mutated, alter binding to G␣ q/ll . These mutations do not alter the ability of full-length GRK2 to phosphorylate rhodopsin, an activity that also requires the amino-terminal domain. Mutations causing G␣ q/ll binding defects impair recruitment to the plasma membrane by activated G␣ q and regulation of G␣ q -stimulated phospholipase C␤ activity when introduced into full-length GRK2. Two different protein interaction sites have previously been identified on RH domains. The G␣ binding sites on RGS4 and RGS9, called the "A" site, is localized to the loops between helices ␣3 and ␣4, ␣5 and ␣6, and ␣7 and ␣8. The adenomatous polyposis coli (APC) binding site of axin involves residues on ␣ helices 3, 4, and 5 (the "B" site) of its RH domain. We demonstrate that the G␣ q/ll binding site on the GRK2 RH domain is distinct from the "A" and "B" sites and maps primarily to the COOH terminus of its ␣5 helix. We suggest that this novel protein interaction site on an RH domain be designated the "C" site.

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“…AKAP10 can bind to both RI and RII subunit isoforms of PKA, through an interaction with an N-terminal four-helix bundle (dimerization/ docking, D/D domain) in the R subunit dimer of PKA [3,4]. The domain organization of AKAP10 is quite unique, containing two tandem, putative RGS domains, a PKA-binding motif, and a PDZ (PSD95/Dlg/ZO1)-binding motif [5][6][7][8]. These domains provide an element of spatial and temporal coordination between upstream cAMP/PKA signalling events and downstream AKAP-mediated signalling events.…”

Section: Introductionmentioning

confidence: 99%

A-Kinase Anchoring Proteins 10 Expression in Relation to 2073A/G Polymorphism and Tumor Progression in Patients with Colorectal Cancer

Wang

Zhang

Wang

et al. 2013

Pathol. Oncol. Res.

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The cAMP/PKA signalling events regulated by A-kinase anchoring proteins 10 (AKAP10) is involved in tumorigenesis. Previous study showed that AKAP10 polymorphism (2073 A/G, I646V) was associated with colorectal cancer risk. However, there was no literature reporting the role of AKAP10 in the pathogenesis of colorectal cancer. The aim of the study was to investigate the clinicopathologic significance of A-kinase anchoring proteins 10 (AKAP 10) expression and the relationship with its polymorphism in colorectal cancer. The expression of AKAP10 was determined by immunohistochemical staining (IHC) and western blot assay on colorectal cancer (n=176), adenoma (n=87) and distant normal mucosa (n=72). 176 patients with colorectal cancer were genotyped for AKAP10 2073A/G polymorphism by TaqMan RT-PCR. We found that the positive expression rate of AKAP10 in colorectal cancer (59%) was significantly higher than those in adenoma (39%) and distant normal mucosa (42%) (P=0.004). There was no significant difference between adenoma and distant normal mucosa (P=0.741). Positive AKAP10 staining was correlated with deeper tumor invasion (P<0.001)), lymph nodes metastasis (P=0.022), advanced tumor stage (P<0.001) and poorly differentiated degree (P=0.003). Compared with AA genotype (52%), positive expression of AKAP10 was significantly increased in colorectal cancer patients with the variant (AG+GG) genotypes (68%, P=0.033). It was concluded that AKAP10 may play an important role in the development and progression of colorectal cancer.

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Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein

Cited by 93 publications

References 49 publications

Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)

Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)

G Protein-coupled Receptor Kinase 2/Gαq/11 Interaction

A-Kinase Anchoring Proteins 10 Expression in Relation to 2073A/G Polymorphism and Tumor Progression in Patients with Colorectal Cancer

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