Evidence map›Paper›PMID 25527497›Full record

ArticleThe Journal of biological chemistry2015

PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402.

Liesbeth Aerts, Katleen Craessaerts, Bart De Strooper, Vanessa A Morais

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
5.1field-weighted citation impact, top 5% 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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 115 citations in OpenAlex.

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  14. PINK1 is a target of T cell responses in Parkinson's disease.bioRxiv : the preprint server for biology · 2024
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12 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Liesbeth AertsFrom the Center for the Biology of Disease, Flemish Institute for Biotechnology (VIB) and Center for Human Genetics, Leuven Institute for Neurodegenerative Disorders and University Hospitals Leuven, University of Leuven, 3000 Leuven, Belgium and.
Katleen CraessaertsFrom the Center for the Biology of Disease, Flemish Institute for Biotechnology (VIB) and Center for Human Genetics, Leuven Institute for Neurodegenerative Disorders and University Hospitals Leuven, University of Leuven, 3000 Leuven, Belgium and.
Bart De StrooperFrom the Center for the Biology of Disease, Flemish Institute for Biotechnology (VIB) and Center for Human Genetics, Leuven Institute for Neurodegenerative Disorders and University Hospitals Leuven, University of Leuven, 3000 Leuven, Belgium and the University College London, Institute of Neurology, Queen Square, London WC1N 3BG, United Kingdom.
Vanessa A MoraisFrom the Center for the Biology of Disease, Flemish Institute for Biotechnology (VIB) and Center for Human Genetics, Leuven Institute for Neurodegenerative Disorders and University Hospitals Leuven, University of Leuven, 3000 Leuven, Belgium and Vanessa.Morais@cme.vib-kuleuven.be.
KU Leuven · BEUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in the PINK1 gene cause early-onset recessive Parkinson disease. PINK1 is a mitochondrially targeted kinase that regulates multiple aspects of mitochondrial biology, from oxidative phosphorylation to mitochondrial clearance. PINK1 itself is also phosphorylated, and this might be linked to the regulation of its multiple activities. Here we systematically analyze four previously identified phosphorylation sites in PINK1 for their role in autophosphorylation, substrate phosphorylation, and mitophagy. Our data indicate that two of these sites, Ser-228 and Ser-402, are autophosphorylated on truncated PINK1 but not on full-length PINK1, suggesting that the N terminus has an inhibitory effect on phosphorylation. We furthermore establish that phosphorylation of these PINK1 residues regulates the phosphorylation of the substrates Parkin and Ubiquitin. Especially Ser-402 phosphorylation appears to be important for PINK1 function because it is involved in Parkin recruitment and the induction of mitophagy. Finally, we identify Thr-313 as a residue that is critical for PINK1 catalytic activity, but, in contrast to previous reports, we find no evidence that this activity is regulated by phosphorylation. These data clarify the regulation of PINK1 through multisite phosphorylation.

Indexed as

HumansMitochondriaMitochondrial MembranesPhosphorylationProtein KinasesPTEN-Induced Putative KinaseSerineUbiquitinUbiquitin-Protein Ligasesparkin proteinProtein KinasesPTEN-Induced Putative KinaseSerineUbiquitinUbiquitin-Protein LigasesMitochondriaNeurodegenerative DiseaseParkinson DiseasePosttranslational Modification (PTM)Protein PhosphorylationPTEN-induced Putative Kinase 1 (PINK1)Serine/Threonine Protein Kinase

Identifiers

PMID25527497
PMCPMC4317039
OpenAlexW2082868693

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.