Evidence map›Paper›PMID 31602805›Full record

ArticleEMBO reports2019

Parkin-mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes.

Fumika Koyano, Koji Yamano, Hidetaka Kosako, Yoko Kimura, Mayumi Kimura, Yukio Fujiki, Keiji Tanaka, Noriyuki Matsuda

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.5field-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

38 citing papers in PubMed, 55 citations in OpenAlex.

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  14. AAA+ ATPase chaperone p97/VCPNature communications · 2024
    Article
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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

8 authors at 4 institutions in 1 country.

Fumika KoyanoUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Koji YamanoUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima, Japan.
Yoko KimuraDepartment of Agriculture Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, Japan.
Mayumi KimuraUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Yukio FujikiMedical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Japan.
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Noriyuki MatsudaUbiquitin Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.ORCID 0000-0001-8199-952X
Tokyo Metropolitan Institute of Medical Science · JPKyushu University · JPShizuoka University · JPTokushima University · JP

Funding

JSPS KAKENHI JP15K19037JSPS KAKENHI JP15K21743JSPS KAKENHI JP16K18545JSPS KAKENHI JP17H03675JSPS KAKENHI JP17K08635JSPS KAKENHI JP18H02443JSPS KAKENHI JP18H05500JSPS KAKENHI JP18K06237JSPS KAKENHI JP18K14708JSPS KAKENHI JP26000014JSPS KAKENHI JP26116007Ohsumi Frontier Science Foundationthe Chieko Iwanaga Fund for Parkinson's Disease Researchthe Joint Usage and Joint Research Programs, the Institute of Advanced Medical Sciencesthe Takeda Science Foundation
6 · The paper itself

Abstract

Ubiquitylation of outer mitochondrial membrane (OMM) proteins is closely related to the onset of familial Parkinson's disease. Typically, a reduction in the mitochondrial membrane potential results in Parkin-mediated ubiquitylation of OMM proteins, which are then targeted for proteasomal and mitophagic degradation. The role of ubiquitylation of OMM proteins with non-degradative fates, however, remains poorly understood. In this study, we find that the mitochondrial E3 ubiquitin ligase MITOL/March5 translocates from depolarized mitochondria to peroxisomes following mitophagy stimulation. This unusual redistribution is mediated by peroxins (peroxisomal biogenesis factors) Pex3/16 and requires the E3 ligase activity of Parkin, which ubiquitylates K268 in the MITOL C-terminus, essential for p97/VCP-dependent mitochondrial extraction of MITOL. These findings imply that ubiquitylation directs peroxisomal translocation of MITOL upon mitophagy stimulation and reveal a novel role for ubiquitin as a sorting signal that allows certain specialized proteins to escape from damaged mitochondria.

Indexed as

HCT116 CellsHEK293 CellsHeLa CellsHumansMembrane ProteinsMitochondriaMitophagyPeroxinsPeroxisomesProtein TransportUbiquitinationUbiquitin-Protein LigasesValosin Containing ProteinMARCHF5 protein, humanMembrane Proteinsparkin proteinPeroxinsUbiquitin-Protein LigasesValosin Containing ProteinMarch5peroxinPINK1- and Parkin-mediated mitophagyubiquitinVCP

Identifiers

PMID31602805
PMCPMC6893362
OpenAlexW2979332011

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.