Evidence map›Paper›PMID 30131341›Full record

ArticleThe Journal of biological chemistry2018

MAPK15 is part of the ULK complex and controls its activity to regulate early phases of the autophagic process.

David Colecchia, Francesca Dapporto, Serena Tronnolone, Laura Salvini, Mario Chiariello

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.0field-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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.

  1. Guideline
  2. Article
  3. MAPK15 PreventsInternational journal of molecular sciences · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Autophagy dark genes: Can we find them with machine learning?Natural sciences (Weinheim, Germany) · 2023
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

5 authors at 3 institutions in 1 country.

David ColecchiaFrom the Consiglio Nazionale delle Ricerche (CNR), Istituto di Fisiologia Clinica (IFC), Siena 53100.ORCID 0000-0002-0364-8924
Francesca Dapportothe Istituto per lo Studio, la Prevenzione e la Rete Oncologica (ISPRO), Core Research Laboratory (CRL), Unit "Signal Transduction," Siena 53100.
Serena Tronnolonethe Istituto per lo Studio, la Prevenzione e la Rete Oncologica (ISPRO), Core Research Laboratory (CRL), Unit "Signal Transduction," Siena 53100.
Laura Salvinithe Toscana Life Sciences Foundation, Siena 53100, Italy.
Mario ChiarielloFrom the Consiglio Nazionale delle Ricerche (CNR), Istituto di Fisiologia Clinica (IFC), Siena 53100, mario.chiariello@cnr.it.ORCID 0000-0001-8434-5177
Istituto per lo Studio e la Prevenzione Oncologica · ITToscana Life Sciences · ITUniversity of Siena · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy, a pathway for bulk protein degradation and removal of damaged organelles, represents one of the major responses of cells to stress, thereby exerting a strict control on their correct functioning. Consequently, this process has been involved in the pathogenesis and therapeutic responses of several human diseases. Mitogen-activated protein (MAP) kinase 15 (MAPK15) is an atypical member of the MAP kinase family that recently emerged as a key modulator of autophagy and, through this, of cell transformation. Still, no information is available about signaling pathways mediating the effect of MAPK15 on this process, nor is it known which phase of autophagosome biogenesis is affected by this MAP kinase. Here, we demonstrate that MAPK15 stimulated 5'-AMP-activated protein kinase-dependent activity of UNC-51-like kinase 1 (ULK1), the only protein kinase among the ATG-related proteins, toward downstream substrates and signaling intermediates. Importantly, MAPK15 directly interacted with the ULK1 complex and mediated ULK1 activation induced by starvation, a classical stimulus for the autophagic process. In turn, ULK1 and its highly homologous protein ULK2 are able to transduce MAPK15 signals stimulating early phases of autophagosomal biogenesis in a multikinase cascade that offers numerous potential targets for future therapeutic intervention in cancer and other autophagy-related human diseases.

Indexed as

AutophagosomesAutophagyAutophagy-Related Protein-1 HomologDown-RegulationExtracellular Signal-Regulated MAP KinasesHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesPhosphorylationProtein Serine-Threonine KinasesRNA, Small InterferingSignal TransductionAutophagy-Related Protein-1 HomologExtracellular Signal-Regulated MAP KinasesIntracellular Signaling Peptides and ProteinsMAPK15 protein, humanMultiprotein ComplexesProtein Serine-Threonine KinasesRNA, Small InterferingULK1 protein, humanUlk2 protein, humanautophagycell signalingmitogen-activated protein kinase (MAPK)traffickingvesicles

Identifiers

PMID30131341
PMCPMC6187625
OpenAlexW2888281041

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.