Evidence map›Paper›PMID 21103907›Full record

ArticleCellular and molecular life sciences : CMLS2011

Synphilin-1 inhibits alpha-synuclein degradation by the proteasome.

Beatriz Alvarez-Castelao, José G Castaño

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. An Overview of Epigenetic Changes in the Parkinson's Disease Brain.International journal of molecular sciences · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Synphilin-1 Interacts with AMPK and Increases AMPK Phosphorylation.International journal of molecular sciences · 2020
    Article
  10. Article
  11. Protein Partners of α-Synuclein in Health and Disease.Brain pathology (Zurich, Switzerland) · 2016
    Review
  12. Alpha-synuclein structure, functions, and interactions.Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences · 2016
    Review
  13. From intrinsically disordered protein to context-dependent folding: The α-synuclein tetramer is teased out of hiding.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

Beatriz Alvarez-CastelaoDepartamento de Bioquímica, Instituto de Investigaciones Biomédicas Alberto Sols, Universidad Autónoma de Madrid y Consejo Superior de Investigaciones Científicas (UAM-CSIC), Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED) and Idipaz, Facultad de Medicina UAM, 28029, Madrid, Spain.
José G Castaño
Unidades Centrales Científico-Técnicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intracellular deposits of aggregated alpha-synuclein are a hallmark of Parkinson's disease. Protein-protein interactions are critical in the regulation of cell proteostasis. Synphilin-1 interacts both in vitro and in vivo with alpha-synuclein promoting its aggregation. We report here that synphilin-1 specifically inhibits the degradation of alpha-synuclein wild-type and its missense mutants by the 20S proteasome due at least in part by the interaction of the ankyrin and coiled-coil domains of synphilin-1 (amino acids 331-555) with the N-terminal region (amino acids 1-60) of alpha-synuclein. Co-expression of synphilin-1 and alpha-synuclein wild-type in HeLa and N2A cells produces a specific increase in the half-life of alpha-synuclein, as degradation of unstable fluorescent reporters is not affected. Synphilin-1 inhibition can be relieved by co-expression of Siah-1 that targets synphilin-1 to degradation. Synphilin-1 inhibition of the proteasomal pathway of degradation of alpha-synuclein may help to understand the pathophysiological changes occurring in PD and other synucleinopathies.

Indexed as

alpha-SynucleinAnimalsCarrier ProteinsCells, CulturedDose-Response Relationship, DrugDown-RegulationHeLa CellsHumansMutation, MissenseNerve Tissue ProteinsProteasome Endopeptidase ComplexProteasome InhibitorsProtein Processing, Post-TranslationalRatsSubstrate Specificityalpha-SynucleinCarrier ProteinsNerve Tissue ProteinsProteasome Endopeptidase ComplexProteasome InhibitorsSNCAIP protein, human

Identifiers

PMID21103907
PMCPMC11114841
OpenAlexW2045825179

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.