Evidence map›Paper›PMID 39268917›Full record

ReviewEssays in biochemistry2024

CaMKK2: bridging the gap between Ca2+ signaling and energy-sensing.

Luke M McAloon, Abbey G Muller, Kevin Nay, Eudora L Lu, Benoit Smeuninx, Anthony R Means, Mark A Febbraio, John W Scott

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

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  12. Genetic adaptations shaping survival, pregnancy, and life at high altitude and sea level.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
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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

8 authors.

Luke M McAloonDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.
Abbey G MullerDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.
Kevin NayDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.
Eudora L LuDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.
Benoit SmeuninxDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.
Anthony R MeansMolecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, U.S.A.
Mark A FebbraioDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.
John W ScottDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Parkville, Victoria 3052, Australia.ORCID 0000-0002-1896-9798

Funding

Australian Research Council (ARC) DP210102840National Health and Medical Research Council (NHMRC) 2001817
6 · The paper itself

Abstract

Calcium (Ca2+) ions are ubiquitous and indispensable signaling messengers that regulate virtually every cell function. The unique ability of Ca2+ to regulate so many different processes yet cause stimulus specific changes in cell function requires sensing and decoding of Ca2+ signals. Ca2+-sensing proteins, such as calmodulin, decode Ca2+ signals by binding and modifying the function of a diverse range of effector proteins. These effectors include the Ca2+-calmodulin dependent protein kinase kinase-2 (CaMKK2) enzyme, which is the core component of a signaling cascade that plays a key role in important physiological and pathophysiological processes, including brain function and cancer. In addition to its role as a Ca2+ signal decoder, CaMKK2 also serves as an important junction point that connects Ca2+ signaling with energy metabolism. By activating the metabolic regulator AMP-activated protein kinase (AMPK), CaMKK2 integrates Ca2+ signals with cellular energy status, enabling the synchronization of cellular activities regulated by Ca2+ with energy availability. Here, we review the structure, regulation, and function of CaMKK2 and discuss its potential as a treatment target for neurological disorders, metabolic disease, and cancer.

Indexed as

Calcium-Calmodulin-Dependent Protein Kinase KinaseCalcium SignalingEnergy MetabolismAMP-Activated Protein KinasesAnimalsCalciumHumansNeoplasmsAMP-Activated Protein KinasesCalciumCalcium-Calmodulin-Dependent Protein Kinase KinaseCAMKK2 protein, humanAMPKcalcium signalingcalmodulinCaMKK2energy-sensing

Identifiers

PMID39268917
PMCPMC11576191

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.