Evidence map›Paper›PMID 36230985›Full record

ArticleCells2022

Modulatory Role of TPPP3 in Microtubule Organization and Its Impact on Alpha-Synuclein Pathology.

Judit Oláh, Attila Lehotzky, Tibor Szénási, Tímea Berki, Judit Ovádi

Open access · goldAbstract read
In one paragraph

Article in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Proteomic Signatures of ProtectedmedRxiv : the preprint server for health sciences · 2026
    Article
  4. In Vivo Screen of Parkinson's Disease GWAS Risk Genes IdentifiesThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
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  7. Review
  8. Review
  9. 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

5 authors at 2 institutions in 1 country.

Judit OláhInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0002-2470-8631
Attila LehotzkyInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0001-5235-1812
Tibor SzénásiInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Tímea BerkiDepartment of Immunology and Biotechnology, Medical School, University of Pécs, 7624 Pécs, Hungary.
Judit OvádiInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0002-3420-682X
Institute of Molecular Life Sciences · HUUniversity of Pecs · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Parkinson's disease is characterized by locomotion deficits, dopaminergic neuronal loss and alpha-synuclein (SYN) aggregates; the Tubulin Polymerization Promoting Protein (TPPP/p25 or TPPP1) is also implicated in these processes. The moonlighting and chameleon TPPP1 modulates the dynamics/stability of the multifunctional microtubule network by promoting its acetylation and bundling. Previously, we identified the microtubule-associated TPPP3, a homologue of TPPP1 lacking its N-terminus; however, its involvement in physiological or pathological processes was not elucidated. In this work, we have shown the modulatory role of TPPP3, similarly to TPPP1, in microtubule organization, as well as its homo- and hetero-associations with TPPP1. TPPP3, in contrast to TPPP1, virtually does not bind to SYN; consequently, it does not promote SYN aggregation. Its anti-aggregative potency is achieved by counteracting the formation of the TPPP1-SYN pathological complex/aggregation leading to Parkinsonism. The interactions of TPPP3 have been determined and quantified in vitro with recombinant human proteins, cell extracts and in living human cells using different methods including bifunctional fluorescence complementation. The tight association of TPPP3 with TPPP1, but not with SYN, may ensure a unique mechanism for its inhibitory effect. TPPP3 or its selected fragments may become a leading agent for developing anti-Parkinson agents.

Indexed as

alpha-SynucleinParkinson DiseaseCell ExtractsCytoskeletal ProteinsHumansMicrotubulesRecombinant ProteinsTubulinalpha-SynucleinCell ExtractsCytoskeletal ProteinsRecombinant ProteinsSNCA protein, humanTPPP3 protein, humanTubulinalpha-synucleinbrainmicrotubuleParkinsonismpathophysiologyTPPP proteins

Identifiers

PMID36230985
PMCPMC9564178
OpenAlexW4297348608

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.