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Cited by 42Parkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and TherapyNuclear Receptors and Signaling

Restriction of trophic factors and nutrients induces PARKIN expression

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Klinkenberg, M., Gispert, S., Dominguez-Bautista, J. A., Braun, I., Auburger, G., Jendrach, M.·2012·neurogenetics
DOI 10.1007/s10048-011-0303-8PMC PMC3274670
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Abstract

Parkinson's disease (PD) is the most frequent neurodegenerative movement disorder and manifests at old age. While many details of its pathogenesis remain to be elucidated, in particular the protein and mitochondrial quality control during stress responses have been implicated in monogenic PD variants. Especially the mitochondrial kinase PINK1 and the ubiquitin ligase PARKIN are known to cooperate in autophagy after mitochondrial damage. As autophagy is also induced by loss of trophic signaling and PINK1 gene expression is modulated after deprivation of cytokines, we analyzed to what extent trophic signals and starvation stress regulate PINK1 and PARKIN expression. Time course experiments with serum deprivation and nutrient starvation of human SH-SY5Y neuroblastoma cells and primary mouse neurons demonstrated phasic induction of PINK1 transcript up to twofold and PARKIN transcript levels up to sixfold. The corresponding threefold starvation induction of PARKIN protein was limited by its translocation to lysosomes. Analysis of primary mouse cells from PINK1-knockout mice indicated that PARKIN induction and lysosomal translocation occurred independent of PINK1. Suppression of the PI3K-Akt-mTOR signaling by pharmacological agents modulated PARKIN expression accordingly. In conclusion, this expression survey demonstrates that PARKIN and PINK1 are coregulated during starvation and suggest a role of both PD genes in response to trophic signals and starvation stress.

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  • The authors identified 20 targets related to autophagy activation and validated them by qPCR: ATG10, ATG14, ATG16L1, ATG3, ATG4, ATG7, ATG9A, BCL2, GABARAP, GABARAPL1, MAP1LC3B, NBR1, OPTN, PINK1, SQSTM1, ULK1, ULK2, UVRAG, WDR45, WIPI1.

    “In a first case, starting from experimental data available in the literature, we identified 20 targets related to autophagy activation and validated them by qPCR: ATG10, ATG14, ATG16L1, ATG3, ATG4, ATG7, ATG9A, BCL2, GABARAP, GABARAPL1, MAP1LC3B, NBR1, OPTN, PINK1, SQSTM1, ULK1, ULK2, UVRAG, WDR45, WIPI1 (Fig. 2) [18–27].”

    From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [22]

    The Results section describes SQSTM1 as associated with aggregates degraded by autophagy and uses LC3 to monitor autophagosome formation. The Methods section reports qPCR assays for PINK1 and three other genes, not validation of the listed 20-gene panel. The citing authors describe the identification and validation as their own work; this source supports some of the autophagy-related background, but not the full target list. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • The activation list was derived from comparison of publications reporting conditions of gene up-regulation upon autophagy activation.

    “A so called “activation list” has been derived from the comparison of publications, in which we reported conditions of gene up-regulation upon autophagy activation [18–27].”

    From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [22]

  • The restricted "induction list" for the prediction of autophagy activation state is made of 20 targets and was obtained by combining data from previous publications documenting increased mRNA expression following autophagy induction.

    “The restricted “induction list” for the prediction of autophagy activation state, made by 20 targets, was obtained combining data from previous publications [18–27], in which have been documented the increase of the mRNA expression following autophagy induction.”

    From A gene toolbox for monitoring autophagy transcription (2021) · cites this paper as [22]

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Cited by

Sorted by citations

Authors
Klinkenberg, M., Gispert, S., Dominguez-Bautista, J. A., Braun, I., Auburger, G., & Jendrach, M.
Affiliations
Goethe University Frankfurt (DE)
Corresponding author
Jendrach, M.
ORCID
Venue
neurogenetics
Publisher
Springer Science and Business Media LLC
Published
2011-10-26
Volume
13
Issue
1
Pages
9-21
ISSN
  • 1364-6745 (ISSN-L)
  • 1364-6753
DOI
10.1007/s10048-011-0303-8
PMC
PMC3274670
OpenAlex
W2044081873
Cited by
42
References
5
Citations by year
2026: 1 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 2 · 2016: 8 · 2015: 5 · 2014: 7 · 2013: 2 · 2012: 3
FWCI
2.44
Type
journal article
Language
en
Open access
Licence
cc-by-nc
Locations
  • Neurogenetics (publishedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) (submittedVersion, cc-by-nc)
Funders
Bundesministerium für Bildung und Forschung (01GS08138, PTJ 0315584A)
Topics
  • Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Keywords
Parkinson's disease, Parkin, PINK1, trophic signaling, nutrient deprivation, serum deprivation, autophagy, lysosomal translocation, PI3K/AKT/mTOR pathway, mitochondrial quality control, neurodegeneration
MeSH terms
PTEN-Induced Putative Kinase, Animals, Cell Line, Humans, Lysosomes, Parkinson Disease, Protein Kinases, Recombinant Fusion Proteins, Starvation, Mice, Knockout, Intercellular Signaling Peptides and Proteins, Ubiquitin-Protein Ligases, Mice

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