Evidence map›Paper›PMID 34725334›Full record

ArticleCell death & disease2021

CaMKK2 facilitates Golgi-associated vesicle trafficking to sustain cancer cell proliferation.

Lorna M Stewart, Lisa Gerner, Mandy Rettel, Frank Stein, James F Burrows, Ian G Mills, Emma Evergren

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. The role of CaMKK2 in Golgi-associated vesicle trafficking.Biochemical Society transactions · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Novel Insights into Autophagy and Prostate Cancer: A Comprehensive Review.International journal of molecular sciences · 2022
    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

7 authors at 3 institutions in 3 countries.

Lorna M StewartPatrick G Johnston Centre for Cancer Research, Queen's University Belfast, 97 Lisburn Road, Belfast, BT9 7AE, UK.
Lisa GernerNordic EMBL Partnership, Centre for Molecular Medicine Norway (NCMM), University of Oslo, P.O.Box 1137, Blindern, 0318, Oslo, Norway.
Mandy RettelEuropean Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117, Heidelberg, Germany.
Frank SteinEuropean Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117, Heidelberg, Germany.ORCID 0000-0001-9695-1692
James F BurrowsSchool of Pharmacy, Queen's University Belfast, 97 Lisburn Road, Belfast, BT9 7BL, UK.
Ian G Mills *Patrick G Johnston Centre for Cancer Research, Queen's University Belfast, 97 Lisburn Road, Belfast, BT9 7AE, UK. ian.mills@nds.ox.ac.uk.ORCID 0000-0001-5347-5083
Emma Evergren *Patrick G Johnston Centre for Cancer Research, Queen's University Belfast, 97 Lisburn Road, Belfast, BT9 7AE, UK.
Queen's University Belfast · GBEuropean Molecular Biology Laboratory · DEUniversity of Oslo · NO

Funding

Norges Forskningsråd (Research Council of Norway) 230559Prostate Cancer UK CEO13_2- 004
6 · The paper itself

Abstract

Calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2) regulates cell and whole-body metabolism and supports tumorigenesis. The cellular impacts of perturbing CAMKK2 expression are, however, not yet fully characterised. By knocking down CAMKK2 levels, we have identified a number of significant subcellular changes indicative of perturbations in vesicle trafficking within the endomembrane compartment. To determine how they might contribute to effects on cell proliferation, we have used proteomics to identify Gemin4 as a direct interactor, capable of binding CAMKK2 and COPI subunits. Prompted by this, we confirmed that CAMKK2 knockdown leads to concomitant and significant reductions in δ-COP protein. Using imaging, we show that CAMKK2 knockdown leads to Golgi expansion, the induction of ER stress, abortive autophagy and impaired lysosomal acidification. All are phenotypes of COPI depletion. Based on our findings, we hypothesise that CAMKK2 sustains cell proliferation in large part through effects on organelle integrity and membrane trafficking.

Indexed as

AcidsAmino Acid MotifsAmino Acid SequenceAutophagyCalcium-Calmodulin-Dependent Protein Kinase KinaseCell Line, TumorCell ProliferationCoat Protein Complex IConserved SequenceGolgi ApparatusHomeostasisHumansLysosomesMinor Histocompatibility AntigensNeoplasmsPeptidesAcidsCalcium-Calmodulin-Dependent Protein Kinase KinaseCoat Protein Complex IGEMIN4 protein, humanMinor Histocompatibility AntigensPeptidesRibonucleoproteins, Small NuclearRNA, Small Interfering

Identifiers

PMID34725334
PMCPMC8560770
OpenAlexW3209663013

What OpenQuestion holds

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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.