Evidence map›Paper›PMID 26446261›Full record

ArticleJournal of cell science2015

Endocytic membrane turnover at the leading edge is driven by a transient interaction between Cdc42 and GRAF1.

Monika K Francis, Mikkel R Holst, Maite Vidal-Quadras, Sara Henriksson, Rachel Santarella-Mellwig, Linda Sandblad, Richard Lundmark

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Article
  5. Targeting the Inside of Cells with Biologicals: Chemicals as a Delivery Strategy.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Membrane Heterogeneity Controls Cellular Endocytic Trafficking.Frontiers in cell and developmental biology · 2020
    Review
  13. Article
  14. Spoiled for Choice: Diverse Endocytic Pathways Function at the Cell Surface.Annual review of cell and developmental biology · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

7 authors at 2 institutions in 2 countries.

Monika K FrancisIntegrative Medical Biology, Umeå University, Umeå 901 87, Sweden Medical Biochemistry and Biophysics, Umeå University, Umeå 901 87, Sweden.
Mikkel R HolstIntegrative Medical Biology, Umeå University, Umeå 901 87, Sweden.
Maite Vidal-QuadrasIntegrative Medical Biology, Umeå University, Umeå 901 87, Sweden.
Sara HenrikssonMedical Biochemistry and Biophysics, Umeå University, Umeå 901 87, Sweden Molecular Biology, Umeå University, Umeå 901 87, Sweden.
Rachel Santarella-MellwigEuropean Molecular Biology Laboratory, Meyerhofstr. 1, Heidelberg 69 117, Germany.
Linda SandbladMolecular Biology, Umeå University, Umeå 901 87, Sweden.
Richard LundmarkIntegrative Medical Biology, Umeå University, Umeå 901 87, Sweden Medical Biochemistry and Biophysics, Umeå University, Umeå 901 87, Sweden richard.lundmark@umu.se.
Umeå University · SEEuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Changes in cell morphology require coordination of plasma membrane turnover and cytoskeleton dynamics, processes that are regulated by Rho GTPases. Here, we describe how a direct interaction between the Rho GTPase Cdc42 and the GTPase-activating protein (GAP) GRAF1 (also known as ARHGAP26), facilitates rapid cell surface turnover at the leading edge. Both Cdc42 and GRAF1 were required for fluid-phase uptake and regulated the generation of transient GRAF1-coated endocytic carriers, which were distinct from clathrin-coated vesicles. GRAF1 was found to transiently assemble at discrete Cdc42-enriched punctae at the plasma membrane, resulting in a corresponding decrease in the microdomain association of Cdc42. However, Cdc42 captured in its active state was, through a GAP-domain-mediated interaction, localised together with GRAF1 on accumulated internal structures derived from the cell surface. Correlative fluorescence and electron tomography microscopy revealed that these structures were clusters of small membrane carriers with defective endosomal processing. We conclude that a transient interaction between Cdc42 and GRAF1 drives endocytic turnover and controls the transition essential for endosomal maturation of plasma membrane internalised by this mechanism.

Indexed as

Actinscdc42 GTP-Binding ProteinClathrin-Coated VesiclesEndocytosisGTPase-Activating ProteinsHeLa CellsHumansActinsARHGAP26 protein, humancdc42 GTP-Binding ProteinGTPase-Activating ProteinsActinCdc42Cell surfaceClathrin-independent endocytosisGRAF1

Identifiers

PMID26446261
PMCPMC4712783
OpenAlexW2206490697

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.