Evidence map›Paper›PMID 19553474›Full record

ArticleMolecular biology of the cell2009

{alpha}-synuclein and its A30P mutant affect actin cytoskeletal structure and dynamics.

Vítor L Sousa, Serena Bellani, Maila Giannandrea, Malikmohamed Yousuf, Flavia Valtorta, Jacopo Meldolesi, Evelina Chieregatti

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.3field-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

67 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
  2. Neuronal Calcium Signaling and Cytoskeletal Dynamics in Neurodegeneration.International journal of molecular sciences · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. In Silico Neuroprotective Effects of SpecificInternational journal of molecular sciences · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Alpha and Beta Synucleins: From Pathophysiology to Clinical Application as Biomarkers.Movement disorders : official journal of the Movement Disorder Society · 2022
    Review
  14. Review
  15. Article
  16. Fluid markers of synapse degeneration in synucleinopathies.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
  17. Review
  18. Review
  19. Review
  20. The Association between α-Synuclein and α-Tubulin in Brain Synapses.International journal of molecular sciences · 2021
    Article

7 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 1 country.

Vítor L SousaDepartment of Neuroscience, San Raffaele Scientific Institute, Milan, Italy.
Serena Bellani
Maila Giannandrea
Malikmohamed Yousuf
Flavia Valtorta
Jacopo Meldolesi
Evelina Chieregatti
Vita-Salute San Raffaele University · ITSan Raffaele University of Rome · IT

Funding

Telethon GGP05134
6 · The paper itself

Abstract

The function of alpha-synuclein, a soluble protein abundant in the brain and concentrated at presynaptic terminals, is still undefined. Yet, alpha-synuclein overexpression and the expression of its A30P mutant are associated with familial Parkinson's disease. Working in cell-free conditions, in two cell lines as well as in primary neurons we demonstrate that alpha-synuclein and its A30P mutant have different effects on actin polymerization. Wild-type alpha-synuclein binds actin, slows down its polymerization and accelerates its depolymerization, probably by monomer sequestration; A30P mutant alpha-synuclein increases the rate of actin polymerization and disrupts the cytoskeleton during reassembly of actin filaments. Consequently, in cells expressing mutant alpha-synuclein, cytoskeleton-dependent processes, such as cell migration, are inhibited, while exo- and endocytic traffic is altered. In hippocampal neurons from mice carrying a deletion of the alpha-synuclein gene, electroporation of wild-type alpha-synuclein increases actin instability during remodeling, with growth of lamellipodia-like structures and apparent cell enlargement, whereas A30P alpha-synuclein induces discrete actin-rich foci during cytoskeleton reassembly. In conclusion, alpha-synuclein appears to play a major role in actin cytoskeletal dynamics and various aspects of microfilament function. Actin cytoskeletal disruption induced by the A30P mutant might alter various cellular processes and thereby play a role in the pathogenesis of neurodegeneration.

Indexed as

alpha-SynucleinCytoskeletonPoint MutationActinsAnimalsBridged Bicyclo Compounds, HeterocyclicCell MembraneCell MovementCells, CulturedEpithelial CellsHippocampusMiceMice, Inbred C57BLNeuronsProtein BindingPseudopodiaActinsalpha-SynucleinBridged Bicyclo Compounds, Heterocycliclatrunculin AThiazolidines

Identifiers

PMID19553474
PMCPMC2777932
OpenAlexW2086460722

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.