Evidence map›Paper›PMID 15082776›Full record

ArticleMolecular and cellular biology2004

The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p.

Céline Lafourcade, Jean-Marc Galan, Yvonne Gloor, Rosine Haguenauer-Tsapis, Matthias Peter

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Arf1 orchestrates Rab GTPase conversion at theMolecular biology of the cell · 2021
    Article
  2. Off the wall: The rhyme and reason ofCell surface (Amsterdam, Netherlands) · 2019
    Review
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  10. GTPase networks in membrane traffic.Annual review of biochemistry · 2012
    Review
  11. Article
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  15. A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
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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

5 authors at 2 institutions in 2 countries.

Céline LafourcadeSwiss Federal Institute of Technology Zurich (ETH), Institute of Biochemistry, ETH Hoenggerberg, 8093 Zurich, Switzerland.
Jean-Marc Galan
Yvonne Gloor
Rosine Haguenauer-Tsapis
Matthias Peter
ETH Zurich · CHInstitut Jacques Monod · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rab/Ypt GTPases are key regulators of membrane trafficking and together with SNARE proteins mediate selective fusion of vesicles with target compartments. A family of GTPase-activating enzymes (GAPs) specific for Rab/Ypt GTPases has been discovered, but little is known about their function and substrate specificity in vivo. Here we show that the GAP activity of Gyp1p, a yeast member of this family, is specifically required for recycling of the SNARE Snc1p and the membrane dye FM4-64, implying that inactivation of a Rab/Ypt GTPase may be necessary for recycling of membrane material. Interestingly, recycling of GFP-Snc1p in gyp1 Delta cells is partially restored by reducing the activity of Ypt1p. Moreover, GFP-Snc1p accumulated intracellularly in wild-type cells expressing a GTP-locked, mutant form of Ypt1p (Ypt1p-Q67L), suggesting that GTP hydrolysis of Ypt1p is essential for recycling. Ypt6p is known to be required for the fusion of recycling vesicles to the late Golgi compartment. Interestingly, the deletions of GYP1 and YPT6 were synthetic lethal, raising the possibility that at least two distinct pathways are involved in recycling of membrane material.

Indexed as

Amino Acid SequenceAnimalsBiological TransportCell MembraneEndocytosisEndosomesExocytosisFluorescent DyesGolgi ApparatusGTPase-Activating ProteinsHumansMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataPyridinium CompoundsQuaternary Ammonium CompoundsFluorescent DyesFM 4-64GTPase-Activating ProteinsGYP1 protein, S cerevisiaeMembrane ProteinsMembrane Transport ProteinsPyridinium CompoundsQuaternary Ammonium Compoundsrab GTP-Binding ProteinsRecombinant Fusion ProteinsR-SNARE ProteinsSaccharomyces cerevisiae ProteinsSNC1 protein, S cerevisiaeYPT1 protein, S cerevisiae

Identifiers

PMID15082776
PMCPMC387746
OpenAlexW2114736119

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.