Evidence map›Paper›PMID 21812984›Full record

ArticleBMC biochemistry2011

The testis-specific Cα2 subunit of PKA is kinetically indistinguishable from the common Cα1 subunit of PKA.

Maike M Vetter, Hans-M Zenn, Eva Méndez, Heidrun van den Boom, Friedrich W Herberg, Bjørn S Skålhegg

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Article in BMC biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

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0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

13 citing papers in PubMed.

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  4. The Tails of Protein Kinase A.Molecular pharmacology · 2022
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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

6 authors.

Maike M VetterDepartment of Nutrition, Institute of Basic Medical Sciences, University of Oslo, Pb 1046 Blindern, Oslo, Norway.
Hans-M Zenn
Eva Méndez
Heidrun van den Boom
Friedrich W Herberg
Bjørn S Skålhegg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe two variants of the α-form of the catalytic (C) subunit of protein kinase A (PKA), designated Cα1 and Cα2, are encoded by the PRKACA gene. Whereas Cα1 is ubiquitous, Cα2 expression is restricted to the sperm cell. Cα1 and Cα2 are encoded with different N-terminal domains. In Cα1 but not Cα2 the N-terminal end introduces three sites for posttranslational modifications which include myristylation at Gly1, Asp-specific deamidation at Asn2 and autophosphorylation at Ser10. Previous reports have implicated specific biological features correlating with these modifications on Cα1. Since Cα2 is not modified in the same way as Cα1 we tested if they have distinct biochemical activities that may be reflected in different biological properties.

resultsWe show that Cα2 interacts with the two major forms of the regulatory subunit (R) of PKA, RI and RII, to form cAMP-sensitive PKAI and PKAII holoenzymes both in vitro and in vivo as is also the case with Cα1. Moreover, using Surface Plasmon Resonance (SPR), we show that the interaction patterns of the physiological inhibitors RI, RII and PKI were comparable for Cα2 and Cα1. This is also the case for their potency to inhibit catalytic activities of Cα2 and Cα1.

conclusionWe conclude that the regulatory complexes formed with either Cα1 or Cα2, respectively, are indistinguishable.

Indexed as

Catalytic DomainCyclic AMP-Dependent Protein Kinase Catalytic SubunitsCyclic AMP-Dependent Protein Kinase RIalpha SubunitCyclic AMP-Dependent Protein Kinase RIIalpha SubunitCyclic AMP-Dependent Protein KinasesEnzyme ActivationHoloenzymesHumansIsoenzymesMaleOrgan SpecificitySpermatozoaSurface Plasmon ResonanceTestisCyclic AMP-Dependent Protein Kinase Catalytic SubunitsCyclic AMP-Dependent Protein Kinase RIalpha SubunitCyclic AMP-Dependent Protein Kinase RIIalpha SubunitCyclic AMP-Dependent Protein KinasesHoloenzymesIsoenzymesPRKACA protein, human

Identifiers

PMID21812984
PMCPMC3163529

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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.