Evidence map›Paper›PMID 31025544›Full record

ReviewCNS neuroscience & therapeutics2019

Phosphoregulation on mitochondria: Integration of cell and organelle responses.

Maribel Lucero, Ana E Suarez, Jeremy W Chambers

Open access · goldAbstract readReview
In one paragraph

Review in CNS neuroscience & therapeutics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Review
  3. Restoration of pp60International journal of molecular sciences · 2025
    Article
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  5. Regulation of cancer progression by CK2: an emerging therapeutic target.Medical oncology (Northwood, London, England) · 2024
    Review
  6. Article
  7. Article
  8. Carbon dioxide and MAPK signalling: towards therapy for inflammation.Cell communication and signaling : CCS · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Peptidoglycan inhibits beigeing of adipose tissue.Acta pharmaceutica Sinica. B · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Antioxidants (Basel, Switzerland) · 2021
    Article
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.

Maribel LuceroDepartment of Environmental Health Sciences, Robert Stempel College of Public Health & Social Work, the Biomolecular Sciences Institute, Florida International University, Miami, Florida.
Ana E SuarezDepartment of Environmental Health Sciences, Robert Stempel College of Public Health & Social Work, the Biomolecular Sciences Institute, Florida International University, Miami, Florida.
Jeremy W ChambersDepartment of Environmental Health Sciences, Robert Stempel College of Public Health & Social Work, the Biomolecular Sciences Institute, Florida International University, Miami, Florida.ORCID 0000-0002-6143-3091
Florida International University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are highly integrated organelles that are crucial to cell adaptation and mitigating adverse physiology. Recent studies demonstrate that fundamental signal transduction pathways incorporate mitochondrial substrates into their biological programs. Reversible phosphorylation is emerging as a useful mechanism to modulate mitochondrial function in accordance with cellular changes. Critical serine/threonine protein kinases, such as the c-Jun N-terminal kinase (JNK), protein kinase A (PKA), PTEN-induced kinase-1 (PINK1), and AMP-dependent protein kinase (AMPK), readily translocate to the outer mitochondrial membrane (OMM), the interface of mitochondria-cell communication. OMM protein kinases phosphorylate diverse mitochondrial substrates that have discrete effects on organelle dynamics, protein import, respiratory complex activity, antioxidant capacity, and apoptosis. OMM phosphorylation events can be tempered through the actions of local protein phosphatases, such as mitogen-activated protein kinase phosphatase-1 (MKP-1) and protein phosphatase 2A (PP2A), to regulate the extent and duration of signaling. The central mediators of OMM signal transduction are the scaffold proteins because the relative abundance of these accessory proteins determines the magnitude and duration of a signaling event on the mitochondrial surface, which dictates the biological outcome of a local signal transduction pathway. The concentrations of scaffold proteins, such as A-kinase anchoring proteins (AKAPs) and Sab (or SH3 binding protein 5-SH3BP5), have been shown to influence neuronal survival and vulnerability, respectively, in models of Parkinson's disease (PD), highlighting the importance of OMM signaling to health and disease. Despite recent progress, much remains to be discovered concerning the mechanisms of OMM signaling. Nonetheless, enhancing beneficial OMM signaling events and inhibiting detrimental protein-protein interactions on the mitochondrial surface may represent highly selective approaches to restore mitochondrial health and homeostasis and mitigate organelle dysfunction in conditions such as PD.

Indexed as

AnimalsHumansMitochondriaPhosphoric Monoester HydrolasesPhosphorylationPhosphotransferasesSignal TransductionPhosphoric Monoester HydrolasesPhosphotransferasesA-kinase anchoring protienc-Jun N-terminal Kinase (JNK)leucine-rich repeat kinase 2 (LRRK2)outer mitochondrial membraneprotein phosphatasePTEN-induced kinase-1 (PINK-1) mitochondriaSab (SH3-binding protein 5; SH3BP5)

Identifiers

PMID31025544
PMCPMC6566066
OpenAlexW2940949286

What OpenQuestion 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 OpenQuestion graph.