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Cited by 258Alzheimer's disease research and treatmentsProtein Kinase Regulation and GTPase SignalingNeuroscience and Neuropharmacology Research

The Role of p38 MAPK and Its Substrates in Neuronal Plasticity and Neurodegenerative Disease

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Corrêa, Sônia A. L., Eales, Katherine L.·2012·Journal of Signal Transduction
DOI 10.1155/2012/649079PMC PMC3389708
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Abstract

A significant amount of evidence suggests that the p38-mitogen-activated protein kinase (MAPK) signalling cascade plays a crucial role in synaptic plasticity and in neurodegenerative diseases. In this review we will discuss the cellular localisation and activation of p38 MAPK and the recent advances on the molecular and cellular mechanisms of its substrates: MAPKAPK 2 (MK2) and tau protein. In particular we will focus our attention on the understanding of the p38 MAPK-MK2 and p38 MAPK-tau activation axis in controlling neuroinflammation, actin remodelling and tau hyperphosphorylation, processes that are thought to be involved in normal ageing as well as in neurodegenerative diseases. We will also give some insight into how elucidating the precise role of p38 MAPK-MK2 and p38 MAPK-tau signalling cascades may help to identify novel therapeutic targets to slow down the symptoms observed in neurodegenerative diseases such as Alzheimer's and Parkinson's disease.

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  • p38α-mediated cytokine overproduction in microglia has been linked to inflammation-induced neurotoxicity in a variety of mouse models.

    “The p38α-mediated cytokine overproduction in microglia has been linked to inflammation-induced neurotoxicity in a variety of mouse models [22, 27–33].”

    From Selective suppression of the α isoform of p38 MAPK rescues late-stage tau pathology (2016) · cites this paper as [31]

    Section 3.2 links p38 MAPK activation in glial cells to increased inflammatory cytokines and potential neuronal toxicity; it also reports that a selective p38α inhibitor blocks increased inflammatory-molecule production. The neurotoxicity examples described there involve glial cultures and rat brains, not a variety of mouse models. No page numbers are provided in our copy. (LLM, conf=0.87)

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Authors
Corrêa, S. A. L., & Eales, K. L.
Affiliations
University of Warwick (GB)
Corresponding author
Corrêa, Sônia A. L.
ORCID
Venue
Journal of Signal Transduction
Publisher
Wiley
Published
2012-06-25
Volume
2012
Pages
1-12
ISSN
  • 2090-1739 (ISSN-L)
  • 2090-1747
DOI
10.1155/2012/649079
PMC
PMC3389708
OpenAlex
W1999970418
Cited by
258
References
10
Citations by year
2026: 16 · 2025: 14 · 2024: 18 · 2023: 18 · 2022: 16 · 2021: 34 · 2020: 26 · 2019: 22 · 2018: 23 · 2017: 19 · 2016: 18 · 2015: 15 · 2014: 9 · 2013: 10
FWCI
7.29
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Signal Transduction (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
Funders
  • Biotechnology and Biological Sciences Research Council (BB/H018344/1, BB/J02127X/1)
  • University of Warwick (BB/H018344/1, BB/J02127X/1)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
p38 MAPK, MAPKAPK2, tau protein, synaptic plasticity, neurodegenerative diseases, neuroinflammation, actin cytoskeleton remodeling, tau hyperphosphorylation, aging, Alzheimer's disease, Parkinson's disease, therapeutic target

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