Evidence map›Paper›PMID 22797896›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Localization and quaternary structure of the PKA RIβ holoenzyme.

Ronit Ilouz, José Bubis, Jian Wu, Yun Young Yim, Michael S Deal, Alexandr P Kornev, Yuliang Ma, Donald K Blumenthal, Susan S Taylor

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

51 citing papers in PubMed, 67 citations in OpenAlex.

  1. Regulation of Translation by PKA Signaling Pathway.International journal of molecular sciences · 2026
    Review
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  6. N3A motifs in RIβ mediate allosteric crosstalk between cAMP and ATP in PKA activation.Protein science : a publication of the Protein Society · 2025
    Article
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  11. Review
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  19. Variants in PRKAR1B cause a neurodevelopmental disorder with autism spectrum disorder, apraxia, and insensitivity to pain.Genetics in medicine : official journal of the American College of Medical Genetics · 2021
    Article
  20. Regulation of Cardiac PKA Signaling by cAMP and Oxidants.Antioxidants (Basel, Switzerland) · 2021
    Review
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

9 authors at 4 institutions in 2 countries.

Ronit IlouzHoward Hughes Medical Institute, and Departments of Chemistry and Biochemistry and Pharmacology, University of California at San Diego, La Jolla, CA 92093, USA.
José Bubis
Jian Wu
Yun Young Yim
Michael S Deal
Alexandr P Kornev
Yuliang Ma
Donald K Blumenthal
Susan S Taylor
Howard Hughes Medical Institute · USSimón Bolívar University · VEUniversity of California, San Diego · USUniversity of Utah · US

Funding

Project# 4: INTERACTIONS OF ANCHORING PROTEINS WITH THEIR TARGETSP01DK054441 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1999 to 2017
$27.3M
Protein Kinase Regulatory Subunit I Directed MutagenesisR01GM034921 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2018
$7.2M
Howard Hughes Medical InstituteNIDDK NIH HHS DK54441NIDDK NIH HHS P01 DK054441NIGMS NIH HHS GM34921NIGMS NIH HHS R01 GM034921
6 · The paper itself

Abstract

Specificity for signaling by cAMP-dependent protein kinase (PKA) is achieved by both targeting and isoform diversity. The inactive PKA holoenzyme has two catalytic (C) subunits and a regulatory (R) subunit dimer (R(2):C(2)). Although the RIα, RIIα, and RIIβ isoforms are well studied, little is known about RIβ. We show here that RIβ is enriched selectively in mitochondria and hypothesized that its unique biological importance and functional nonredundancy will correlate with its structure. Small-angle X-ray scattering showed that the overall shape of RIβ(2):C(2) is different from its closest homolog, RIα(2):C(2). The full-length RIβ(2):C(2) crystal structure allows us to visualize all the domains of the PKA holoenzyme complex and shows how isoform-specific assembly of holoenzyme complexes can create distinct quaternary structures even though the R(1):C(1) heterodimers are similar in all isoforms. The creation of discrete isoform-specific PKA holoenzyme signaling "foci" paves the way for exploring further biological roles of PKA RIβ and establishes a paradigm for PKA signaling.

Indexed as

AnimalsCrystallography, X-RayCyclic AMP-Dependent Protein Kinase RIbeta SubunitHoloenzymesMiceProtein Structure, QuaternarySecond Messenger SystemsStructure-Activity RelationshipCyclic AMP-Dependent Protein Kinase RIbeta SubunitHoloenzymes

Identifiers

PMID22797896
PMCPMC3411989
OpenAlexW2036184042

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.