Evidence map›Paper›PMID 9326583›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain.

L J Huang, K Durick, J A Weiner, J Chun, S S Taylor

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

75 citing papers in PubMed, 216 citations in OpenAlex.

  1. Trial
  2. Regulation of Translation by PKA Signaling Pathway.International journal of molecular sciences · 2026
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15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

L J HuangHoward Hughes Medical Institute, Department of Chemistry and Biochemistry, School of Medicine, University of California at San Diego, La Jolla, CA 92093-0654, USA.
K Durick
J A Weiner
J Chun
S S Taylor
Howard Hughes Medical Institute · US

Funding

GENETIC MECHANISMS AND REGULATIONT32GM007240 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 1985 to 2019
$23.8M
Contemporary Approaches to Cancer Cell Signaling and CommunicationT32CA009523 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DONOGHUE, DANIEL J, YANG, JING · 1985 to 2025
$12.1M
RECEPTOR-MEDIATED LPA SIGNALING IN CORTICAL DEVELOPMENTR01MH051699 · NIMH · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI CHUN, JEROLD · 2001 to 2009
$3.3M
CELL LINES FOR FINDING DEVELOPMENTAL NEOCORTICAL GENESR29MH051699 · NIMH · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI CHUN, JEROLD · 1994 to 1998
–
NCI NIH HHS T32 CA009523NCI NIH HHS T32 CA09523NIGMS NIH HHS 2T32GM07240-21A1NIGMS NIH HHS T32 GM007240NIMH NIH HHS R01 MH051699NIMH NIH HHS R29MH51699
6 · The paper itself

Abstract

Subcellular localization directed by specific A kinase anchoring proteins (AKAPs) is a mechanism for compartmentalization of cAMP-dependent protein kinase (PKA). Using a two-hybrid screen, a novel AKAP was isolated. Because it interacts with both the type I and type II regulatory subunits, it was defined as a dual specific AKAP or D-AKAP1. Here we report the cloning and characterization of another novel cDNA isolated from that screen. This new member of the D-AKAP family, D-AKAP2, also binds both types of regulatory subunits. A message of 5 kb pairs was detected for D-AKAP2 in all embryonic stages and in all adult tissues tested. In brain, skeletal muscle, kidney, and testis, a 10-kb mRNA was identified. In testis, several small mRNAs were observed. Therefore, D-AKAP2 represents a novel family of proteins. cDNA cloning from a mouse testis library identified the full length D-AKAP2. It is composed of 372 amino acids which includes the R binding fragment, residues 333-372, at its C-terminus. Based on coprecipitation assays, the R binding domain interacts with the N-terminal dimerization domain of RIalpha and RIIalpha. A putative RGS domain was identified near the N-terminal region of D-AKAP2. The presence of this domain raises the intriguing possibility that D-AKAP2 may interact with a Galpha protein thus providing a link between the signaling machinery at the plasma membrane and the downstream kinase.

Indexed as

Adaptor Proteins, Signal TransducingProteinsA Kinase Anchor ProteinsAmino Acid SequenceAnimalsBase SequenceBinding SitesCarrier ProteinsCloning, MolecularConserved SequenceCyclic AMP-Dependent Protein Kinase RIalpha SubunitCyclic AMP-Dependent Protein Kinase RIIalpha SubunitCyclic AMP-Dependent Protein KinasesCyclic AMP-Dependent Protein Kinase Type IIDNA, ComplementaryEmbryo, MammalianAdaptor Proteins, Signal TransducingAkap10 protein, mouseA Kinase Anchor ProteinsCarrier ProteinsCyclic AMP-Dependent Protein Kinase RIalpha SubunitCyclic AMP-Dependent Protein Kinase RIIalpha SubunitCyclic AMP-Dependent Protein KinasesCyclic AMP-Dependent Protein Kinase Type IIDNA, ComplementaryGTPase-Activating ProteinsMacromolecular SubstancesPrkar1a protein, mousePrkar2a protein, mouseProteinsRecombinant ProteinsRNA, Messenger

Identifiers

PMID9326583
PMCPMC23409
OpenAlexW2171041527

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.