Evidence map›Paper›PMID 29991771›Full record

ArticleScientific reports2018

Structural insights into ubiquitin phosphorylation by PINK1.

Kei Okatsu, Yusuke Sato, Koji Yamano, Noriyuki Matsuda, Lumi Negishi, Akiko Takahashi, Atsushi Yamagata, Sakurako Goto-Ito, Masaki Mishima, Yutaka Ito and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Cytosolic Delivery of Functional Ubiquitin.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  7. Review
  8. Reading and Writing the Ubiquitin Code Using Genetic Code Expansion.Chembiochem : a European journal of chemical biology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Mitophagy and Neurodegeneration: Between the Knowns and the Unknowns.Frontiers in cell and developmental biology · 2022
    Review
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

13 authors at 7 institutions in 2 countries.

Kei OkatsuInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Yusuke SatoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Koji YamanoTokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Noriyuki MatsudaTokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Lumi NegishiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Akiko TakahashiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Atsushi YamagataInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Sakurako Goto-ItoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Masaki MishimaGraduate School of Science & Engineering, Tokyo Metropolitan University, Tokyo, 192-0397, Japan.
Yutaka ItoGraduate School of Science & Engineering, Tokyo Metropolitan University, Tokyo, 192-0397, Japan.ORCID 0000-0002-1030-4660
Toshihiko OkaDepartment of Life Science, Rikkyo University, Tokyo, 171-8501, Japan.
Keiji TanakaTokyo Metropolitan Institute of Medical Science, Tokyo, 156-8506, Japan.
Shuya FukaiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan. fukai@iam.u-tokyo.ac.jp.ORCID 0000-0002-1241-1443
Japan Synchrotron Radiation Research Institute · JPThe University of Tokyo · JPTokyo Metropolitan Institute of Medical Science · JPTokyo Metropolitan University · JPJapan Science and Technology Agency · JPQuantitative BioSciences · USRikkyo University · JP

Funding

Japan Science and Technology Agency (JST) PRESTOJapan Society for the Promotion of Science (JSPS) 17H05888Japan Society for the Promotion of Science (JSPS) JP15H01175Japan Society for the Promotion of Science (JSPS) JP15J10559Japan Society for the Promotion of Science (JSPS) JP16K18545Japan Society for the Promotion of Science (JSPS) JP24247014Japan Society for the Promotion of Science (JSPS) JP24687012Japan Society for the Promotion of Science (JSPS) JP26000014JST | Core Research for Evolutional Science and Technology (CREST) JPMJCR12M5JST | Core Research for Evolutional Science and Technology (CREST) JPMJCR13M3
6 · The paper itself

Abstract

Mutations of PTEN-induced putative kinase 1 (PINK1) and the E3 ubiquitin (Ub) ligase parkin can cause familial parkinsonism. These two proteins are essential for ubiquitylation of damaged mitochondria and subsequent degradation. PINK1 phosphorylates Ser65 of Ub and the Ub-like (UBL) domain of parkin to allosterically relieve the autoinhibition of parkin. To understand the structural mechanism of the Ub/UBL-specific phosphorylation by PINK1, we determined the crystal structure of Tribolium castaneum PINK1 kinase domain (TcPINK1) in complex with a nonhydrolyzable ATP analogue at 2.5 Å resolution. TcPINK1 consists of the N- and C-terminal lobes with the PINK1-specific extension. The ATP analogue is bound in the cleft between the N- and C-terminal lobes. The adenine ring of the ATP analogue is bound to a hydrophobic pocket, whereas the triphosphate group of the ATP analogue and two coordinated Mg ions interact with the catalytic hydrophilic residues. Comparison with protein kinases A and C (PKA and PKC, respectively) unveils a putative Ub/UBL-binding groove, which is wider than the peptide-binding groove of PKA or PKC to accommodate the globular head of Ub or UBL. Further crosslinking analyses suggested a PINK1-interacting surface of Ub. Structure-guided mutational analyses support the findings from the present structural analysis of PINK1.

Indexed as

Adenosine TriphosphateCrystallography, X-RayHumansMutationParkinsonian DisordersPhosphorylationProtein BindingProtein ConformationProtein DomainsProtein KinasesPTEN-Induced Putative KinaseUbiquitinUbiquitin-Protein LigasesAdenosine Triphosphateparkin proteinProtein KinasesPTEN-Induced Putative KinaseUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID29991771
PMCPMC6039469
OpenAlexW2810457935

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.