Evidence map›Paper›PMID 9755160›Full record

ArticleThe EMBO journal1998

alphaKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle.

K U Bayer, K Harbers, H Schulman

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 138 citations in OpenAlex.

  1. Trial
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  4. Article
  5. Reduced O-GlcNAcylation diminishes cardiomyocyte CaJournal of molecular and cellular cardiology · 2023
    Article
  6. Review
  7. Functional implications of CaMKII alternative splicing.The European journal of neuroscience · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Compartmentation of βBritish journal of pharmacology · 2021
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Vascular CaMKII: heart and brain in your arteries.American journal of physiology. Cell physiology · 2016
    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

3 authors at 1 institution in 1 country.

K U BayerDepartment of Neurobiology, Stanford University School of Medicine, 299 Campus Drive, Stanford, CA 94305-5125, USA.
K Harbers
H Schulman
Stanford University · US

Funding

MULTIFUNCTIONAL CA++/CALMODULIN-DEPENDENT PROTEIN KINASER01GM040600 · NIGMS · STANFORD UNIVERSITY · PI SCHULMAN, HOWARD · 1988 to 2001
$573k
NIGMS NIH HHS GM40600
6 · The paper itself

Abstract

Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) is present in a membrane-bound form that phosphorylates synapsin I on neuronal synaptic vesicles and the ryanodine receptor at skeletal muscle sarcoplasmic reticulum (SR), but it is unclear how this soluble enzyme is targeted to membranes. We demonstrate that alphaKAP, a non-kinase protein encoded by a gene within the gene of alpha-CaM kinase II, can target the CaM kinase II holoenzyme to the SR membrane. Our results indicate that alphaKAP (i) is anchored to the membrane via its N-terminal hydrophobic domain, (ii) can co-assemble with catalytically competent CaM kinase II isoforms and target them to the membrane regardless of their state of activation, and (iii) is co-localized and associated with rat skeletal muscle CaM kinase II in vivo. alphaKAP is therefore the first demonstrated anchoring protein for CaM kinase II. CaM kinase II assembled with alphaKAP retains normal enzymatic activity and the ability to become Ca2+-independent following autophosphorylation. A new variant of beta-CaM kinase II, termed betaM-CaM kinase II, is one of the predominant CaM kinase II isoforms associated with alphaKAP in skeletal muscle SR.

Indexed as

Amino Acid SequenceAnimalsBiological TransportCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Carrier ProteinsCell CompartmentationEnzymes, ImmobilizedIsoenzymesMiceMicrosomesModels, BiologicalMolecular Sequence DataProtein BindingRatsSarcoplasmic ReticulumCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Carrier ProteinsEnzymes, ImmobilizedIsoenzymes

Identifiers

PMID9755160
PMCPMC1170888
OpenAlexW2142148418

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.