Evidence map›Paper›PMID 25380047›Full record

ArticlePloS one2014

Septin6 and Septin7 GTP binding proteins regulate AP-3- and ESCRT-dependent multivesicular body biogenesis.

Sofia Traikov, Christoph Stange, Thomas Wassmer, Perrine Paul-Gilloteaux, Jean Salamero, Graça Raposo, Bernard Hoflack

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

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  15. Article
  16. The Mammalian Septin Interactome.Frontiers in cell and developmental biology · 2017
    Review
  17. Article
  18. Article
  19. Septins As Modulators of Endo-Lysosomal Membrane Traffic.Frontiers in cell and developmental biology · 2016
    Review
  20. Septin Mutations in Human Cancers.Frontiers in cell and developmental biology · 2016
    Review
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 3 countries.

Sofia TraikovBiotechnological Center, Technische Universität Dresden, Dresden, Germany.
Christoph StangeBiotechnological Center, Technische Universität Dresden, Dresden, Germany.
Thomas WassmerBiotechnological Center, Technische Universität Dresden, Dresden, Germany; School of Life and Health Sciences, Aston University, Birmingham, United Kingdom.
Perrine Paul-GilloteauxMolecular Mechanisms of Intracellular Transport Laboratory, CNRS-Institut Curie, Paris, France; Cell and Tissue Imaging Facility, PICT-IBiSA & Nikon Imaging Center, CNRS-Institut Curie, Paris, France.
Jean SalameroMolecular Mechanisms of Intracellular Transport Laboratory, CNRS-Institut Curie, Paris, France; Cell and Tissue Imaging Facility, PICT-IBiSA & Nikon Imaging Center, CNRS-Institut Curie, Paris, France.
Graça RaposoMolecular Mechanisms of Intracellular Transport Laboratory, CNRS-Institut Curie, Paris, France.
Bernard HoflackBiotechnological Center, Technische Universität Dresden, Dresden, Germany.
TU Dresden · DEAston University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septins (SEPTs) form a family of GTP-binding proteins implicated in cytoskeleton and membrane organization, cell division and host/pathogen interactions. The precise function of many family members remains elusive. We show that SEPT6 and SEPT7 complexes bound to F-actin regulate protein sorting during multivesicular body (MVB) biogenesis. These complexes bind AP-3, an adapter complex sorting cargos destined to remain in outer membranes of maturing endosomes, modulate AP-3 membrane interactions and the motility of AP-3-positive endosomes. These SEPT-AP interactions also influence the membrane interaction of ESCRT (endosomal-sorting complex required for transport)-I, which selects ubiquitinated cargos for degradation inside MVBs. Whereas our findings demonstrate that SEPT6 and SEPT7 function in the spatial, temporal organization of AP-3- and ESCRT-coated membrane domains, they uncover an unsuspected coordination of these sorting machineries during MVB biogenesis. This requires the E3 ubiquitin ligase LRSAM1, an AP-3 interactor regulating ESCRT-I sorting activity and whose mutations are linked with Charcot-Marie-Tooth neuropathies.

Indexed as

ActinsAdaptor Protein Complex 3Biological TransportCell Cycle ProteinsEndosomal Sorting Complexes Required for TransportHeLa CellsHumansIntracellular MembranesMovementMultivesicular BodiesProtein BindingSeptinsUbiquitin-Protein LigasesActinsAdaptor Protein Complex 3Cell Cycle ProteinsEndosomal Sorting Complexes Required for TransportLRSAM1 protein, humanSEPTIN6 protein, humanSEPTIN7 protein, humanSeptinsUbiquitin-Protein Ligases

Identifiers

PMID25380047
PMCPMC4224394
OpenAlexW1973928848

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.