Evidence map›Paper›PMID 17935997›Full record

ArticleCurrent biology : CB2007

The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology.

Yunli Xie, John P Vessey, Anetta Konecna, Ralf Dahm, Paolo Macchi, Michael A Kiebler

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Current biology : CB, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed, 1 pooled it
6.8field-weighted citation impact, top 2% 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

135 citing papers in PubMed, 1 synthesis or guideline pooled it, 254 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Review
  6. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  7. Article
  8. Review
  9. The MoLfa1 Protein Regulates Fungal Development and Septin Ring Formation inInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Effects ofFrontiers in molecular neuroscience · 2022
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Yunli XieDepartment of Neural Cell Biology, Center for Brain Research, Medical University of Vienna, Vienna A1090, Austria.
John P Vessey
Anetta Konecna
Ralf Dahm
Paolo Macchi
Michael A Kiebler
Medical University of Vienna · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septins, a highly conserved family of GTP-binding proteins, were originally identified in a genetic screen for S. cerevisiae mutants defective in cytokinesis [1, 2]. In yeast, septins maintain the compartmentalization of the yeast plasma membrane during cell division by forming rings at the cortex of the bud neck, and these rings establish a lateral diffusion barrier. In contrast, very little is known about the functions of septins in mammalian cells [3, 4] including postmitotic neurons [5-7]. Here, we show that Septin 7 (Sept7) localizes at the bases of filopodia and at branch points in developing hippocampal neurons. Upon downregulation of Sept7, dendritic branching is impaired. In mature neurons, Sept7 is found at the bases of dendritic spines where it associates with the plasma membrane. Mature Sept7-deficient neurons display elongated spines. Furthermore, Sept5 and Sept11 colocalize with and coimmunoprecipitate with Sept7, thereby arguing for the existence of a Septin5/7/11 complex. Taken together, our findings show an important role for Sept7 in regulating dendritic branching and dendritic-spine morphology. Our observations concur with data from yeast, in which downregulation of septins yields elongated buds, suggesting a conserved function for septins from yeast to mammals.

Indexed as

AnimalsCell Cycle ProteinsCells, CulturedCytoskeletal ProteinsDendritesGTP PhosphohydrolasesHippocampusMultiprotein ComplexesMutationNeuronsPseudopodiaRatsRecombinant ProteinsSeptinsSubcellular FractionsTransfectionCell Cycle ProteinsCytoskeletal ProteinsGTP PhosphohydrolasesMultiprotein ComplexesRecombinant ProteinsSeptin7 protein, ratSeptins

Identifiers

PMID17935997
OpenAlexW1969651353

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.