Evidence map›Paper›PMID 12686590›Full record

ArticleMolecular biology of the cell2003

The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a yeast TGN-to-endosome pathway distinct from the GGA protein-dependent pathway.

Seon-Ah Ha, Javad Torabinejad, Daryll B DeWald, Markus R Wenk, Louise Lucast, Pietro De Camilli, Richard A Newitt, Ruedi Aebersold, Steven F Nothwehr

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Review
  6. Exomer complex regulates protein traffic at the TGN through differential interactions with cargos and clathrin adaptor complexes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  7. Article
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  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. 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

9 authors at 4 institutions in 1 country.

Seon-Ah HaDivision of Biological Sciences, University of Missouri, Columbia, Missouri 65211, USA.
Javad Torabinejad
Daryll B DeWald
Markus R Wenk
Louise Lucast
Pietro De Camilli
Richard A Newitt
Ruedi Aebersold
Steven F Nothwehr
Howard Hughes Medical Institute · USInstitute for Systems Biology · USUniversity of Missouri · USUtah State University · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
ANALYSIS OF GOLGI MEMBRANE PROTEIN LOCALIZATION IN YEASTR01GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 2000 to 2003
$749k
YEAST LATE GOLGI MEMBRANE PROTEIN RETENTIONR29GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 1995 to 1999
–
NCRR NIH HHS P41 RR011823NCRR NIH HHS RR-11823NIGMS NIH HHS GM-53449NIGMS NIH HHS R01 GM053449NIGMS NIH HHS R29 GM053449
6 · The paper itself

Abstract

Yeast TGN resident proteins that frequently cycle between the TGN and endosomes are much more slowly transported to the prevacuolar/late endosomal compartment (PVC) than other proteins. However, TGN protein transport to the PVC is accelerated in mutants lacking function of Inp53p. Inp53p contains a SacI polyphosphoinositide phosphatase domain, a 5-phosphatase domain, and a proline-rich domain. Here we show that all three domains are required to mediate "slow delivery" of TGN proteins into the PVC. Although deletion of the proline-rich domain did not affect general membrane association, it caused localization to become less specific. The proline-rich domain was shown to bind to two proteins, including clathrin heavy chain, Chc1p. Unlike chc1 mutants, inp53 mutants do not mislocalize TGN proteins to the cell surface, consistent with the idea that Chc1p and Inp53p act at a common vesicular trafficking step but that Chc1p is used at other steps also. Like mutations in the AP-1 adaptor complex, mutations in INP53 exhibit synthetic growth and transport defects when combined with mutations in the GGA proteins. Taken together with other recent studies, our results suggest that Inp53p and AP-1/clathrin act together in a TGN-to-early endosome pathway distinct from the direct TGN-to-PVC pathway mediated by GGA/clathrin.

Indexed as

Adaptor Proteins, Vesicular TransportADP-Ribosylation FactorsAmino Acid SequenceBinding SitesBiological Transport, ActiveCarrier ProteinsClathrin Heavy ChainsEndosomesGenes, FungalGolgi ApparatusModels, BiologicalMutationNerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein Structure, TertiarySaccharomyces cerevisiaeAdaptor Proteins, Vesicular TransportADP-Ribosylation FactorsCarrier ProteinsClathrin Heavy ChainsGGA adaptor proteinsINP53 protein, S cerevisiaeNerve Tissue ProteinsPhosphoric Monoester HydrolasesSaccharomyces cerevisiae ProteinssynaptojaninTranscription Factor AP-1

Identifiers

PMID12686590
PMCPMC153103
OpenAlexW2169685408

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.