Evidence map›Paper›PMID 31548421›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Phosphorylation of mitochondrial matrix proteins regulates their selective mitophagic degradation.

Panagiota Kolitsida, Jianwen Zhou, Michal Rackiewicz, Vladimir Nolic, Jörn Dengjel, Hagai Abeliovich

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

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  18. Yeast mitophagy: Unanswered questions.Biochimica et biophysica acta. General subjects · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Panagiota KolitsidaInstitute of Biochemistry, Food Science and Nutrition, Hebrew University of Jerusalem, 7612001 Rehovot, Israel.
Jianwen ZhouDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Michal RackiewiczDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Vladimir NolicInstitute of Biochemistry, Food Science and Nutrition, Hebrew University of Jerusalem, 7612001 Rehovot, Israel.
Jörn DengjelDepartment of Biology, University of Fribourg, 1700 Fribourg, Switzerland.
Hagai AbeliovichInstitute of Biochemistry, Food Science and Nutrition, Hebrew University of Jerusalem, 7612001 Rehovot, Israel; hagai.abeliovich@mail.huji.ac.il.ORCID 0000-0001-7371-4467
University of Fribourg · CHHebrew University of Jerusalem · ILUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitophagy is an important quality-control mechanism in eukaryotic cells, and defects in mitophagy correlate with aging phenomena and neurodegenerative disorders. It is known that different mitochondrial matrix proteins undergo mitophagy with very different rates but, to date, the mechanism underlying this selectivity at the individual protein level has remained obscure. We now present evidence indicating that protein phosphorylation within the mitochondrial matrix plays a mechanistic role in regulating selective mitophagic degradation in yeast via involvement of the Aup1 mitochondrial protein phosphatase, as well as 2 known matrix-localized protein kinases, Pkp1 and Pkp2. By focusing on a specific matrix phosphoprotein reporter, we also demonstrate that phospho-mimetic and nonphosphorylatable point mutations at known phosphosites in the reporter increased or decreased its tendency to undergo mitophagy. Finally, we show that phosphorylation of the reporter protein is dynamically regulated during mitophagy in an Aup1-dependent manner. Our results indicate that structural determinants on a mitochondrial matrix protein can govern its mitophagic fate, and that protein phosphorylation regulates these determinants.

Indexed as

MitophagyMitochondriaMitochondrial ProteinsMutationPhosphoprotein PhosphatasesPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMitochondrial ProteinsPhosphoprotein PhosphatasesProtein KinasesPTC6 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsautophagymitophagyphosphataseprotein phosphorylationSaccharomyces cerevisiae

Identifiers

PMID31548421
PMCPMC6789754
OpenAlexW2976261563

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.