Evidence map›Paper›PMID 22238344›Full record

ArticleThe Journal of biological chemistry2012

Microtubule affinity-regulating kinase 2 (MARK2) turns on phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) at Thr-313, a mutation site in Parkinson disease: effects on mitochondrial transport.

Dorthe Matenia, Cindy Hempp, Thomas Timm, Annika Eikhof, Eva-Maria Mandelkow

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.5field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 66 citations in OpenAlex.

  1. Trial
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Endogenous PTEN-Induced Kinase 1 Regulates Dendritic Architecture and Spinogenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The cell biology of Parkinson's disease.The Journal of cell biology · 2021
    Review
  16. Review
  17. Article
  18. PINK1 Content in Mitochondria is Regulated by ER-Associated Degradation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    Article
  19. Article
  20. Article
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

5 authors at 3 institutions in 1 country.

Dorthe MateniaMax Planck Unit for Structural Molecular Biology, c/o Deutsches Elektronen Synchrotron (DESY), Notkestrasse 85, 22607 Hamburg, Germany. matenia@mpasmb.desy.de
Cindy Hempp
Thomas Timm
Annika Eikhof
Eva-Maria Mandelkow
Deutsches Elektronen-Synchrotron DESY · DEGerman Center for Neurodegenerative Diseases · DEMax Planck Unit for Structural Molecular Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The kinase MARK2/Par-1 plays key roles in several cell processes, including neurodegeneration such as Alzheimer disease by phosphorylating tau and detaching it from microtubules. In search of interaction partners of MARK2, we identified phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1), which is important for the survival of neurons and whose mutations are linked to familial Parkinson disease (PD). MARK2 phosphorylated and activated the cleaved form of PINK1 (ΔN-PINK1; amino acids 156-581). Thr-313 was the primary phosphorylation site, a residue mutated to a non-phosphorylatable form (T313M) in a frequent variant of PD. Mutation of Thr-313 to Met or Glu in PINK1 showed toxic effects with abnormal mitochondrial distribution in neurons. MARK2 and PINK1 were found to colocalize with mitochondria and regulate their transport. ΔN-PINK1 promoted anterograde transport and increased the fraction of stationary mitochondria, whereas full-length PINK1 promoted retrograde transport. In both cases, MARK2 enhanced the effects. The results identify MARK2 as an upstream regulator of PINK1 and ΔN-PINK1 and provide insights into the regulation of mitochondrial trafficking in neurons and neurodegeneration in PD.

Indexed as

Mutation, MissenseAmino Acid SubstitutionAnimalsBiological Transport, ActiveCell SurvivalCHO CellsCricetinaeCricetulusHEK293 CellsHumansMitochondriaNeuronsParkinson DiseasePC12 CellsProtein KinasesProtein Serine-Threonine KinasesMARK2 protein, humanMARK2 protein, ratProtein KinasesProtein Serine-Threonine KinasesPTEN-Induced Putative KinaseThreonine

Identifiers

PMID22238344
PMCPMC3318756
OpenAlexW2072982271

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.