Evidence map›Paper›PMID 33661342›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2021

AMPKα-like proteins as LKB1 downstream targets in cell physiology and cancer.

Ester Molina, Linda Hong, IIana Chefetz

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 24 citations in OpenAlex.

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  9. Role of Liver Kinase 1B in Platelet Activation and Host Defense DuringInternational journal of molecular 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

3 authors at 3 institutions in 2 countries.

Ester MolinaThe Hormel Institute, University of Minnesota, 801 16th Ave NE, Austin, MN, 55912, USA.
Linda HongLoma Linda University School of Medicine, Loma Linda, CA, USA.
IIana ChefetzThe Hormel Institute, University of Minnesota, 801 16th Ave NE, Austin, MN, 55912, USA. ichefetz@umn.edu.ORCID 0000-0002-0975-3311
Hormel (United States) · USLoma Linda University · USUniversity of Minnesota · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the key events in cancer development is the ability of tumor cells to overcome nutrient deprivation and hypoxia. Among proteins performing metabolic adaptation to the various cellular nutrient conditions, liver kinase B 1 (LKB1) and its main downstream target adenosine monophosphate (AMP)-activated protein kinase α (AMPKα) are important sensors of energy requirements within the cell. Although LKB1 was originally described as a tumor suppressor, given its role in metabolism, it potentially acts as a double-edged sword. AMPKα, a master regulator of cell energy demands, is activated when ATP level drops under a certain threshold, responding accordingly through its downstream targets. Twelve downstream kinase targets of LKB1 have been described as AMPKα-like proteins. This group is comprised of novel (nua) kinase family (NUAK) kinases (NUAK1 and 2) linked to cell cycle progression and ultraviolet (UV)-damage; microtubule affinity regulating kinases (MARKs) (MARK1, MARK2, MARK3, and MARK4) that are involved in cell polarity; salt inducible kinases (SIK) (SIK1, SIK2, also known as Qin-induced kinase or QIK and SIK3) that are implicated in cell metabolism and adipose tissue development and mitotic regulation; maternal embryonic leuzine zipper kinase (MELK) that regulate oocyte maturation; and finally brain selective kinases (BRSKs) (BRSK1 and 2), which have been mainly characterized in the brain due to their role in neuronal polarization. Thus, many efforts have been made in order to harness LKB1 kinase and its downstream targets as a possible therapeutic hub in tumor development and propagation. In this review, we describe LKB1 and its downstream target AMPK summarize major functions of various AMPK-like proteins, while focusing on biological functions of BRSK1 and 2 in different models.

Indexed as

AMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesAnimalsCell PolarityEnzyme ActivationHumansMutationNeoplasmsProtein KinasesProtein Serine-Threonine KinasesRepressor ProteinsSignal TransductionAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesMELK protein, humanNUAK1 protein, humanNUAK2 protein, humanProtein KinasesProtein Serine-Threonine KinasesRepressor Proteinssalt-inducible kinase-2, humanSIK1 protein, humanSIK3 protein, humanSTK11 protein, humanAMPKαBRSK1BRSK2LKB1Understudied kinases

Identifiers

PMID33661342
OpenAlexW3134463479

What OpenQuestion holds

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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.