Evidence map›Paper›PMID 16702232›Full record

ArticleThe Journal of cell biology2006

The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast.

Christopher Foote, Steven F Nothwehr

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

  1. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
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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

2 authors at 1 institution in 1 country.

Christopher FooteDivision of Biological Sciences, University of Missouri, Columbia, MO 65211, USA.
Steven F Nothwehr
University of Missouri · US

Funding

MOLECULAR BASIS OF GENE EXPRESSION AND SIGNAL PROCESSINGT32GM008396 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI HANNINK, MARK · 1991 to 2021
$4.1M
ANALYSIS OF GOLGI MEMBRANE PROTEIN LOCALIZATION IN YEASTR01GM053449 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI NOTHWEHR, STEVEN F · 2000 to 2003
$749k
NIGMS NIH HHS 5T32GM008396NIGMS NIH HHS R01 GM053449NIGMS NIH HHS R01GM053449NIGMS NIH HHS T32 GM008396
6 · The paper itself

Abstract

Yeast trans-Golgi network (TGN) membrane proteins maintain steady-state localization by constantly cycling to and from endosomes. In this study, we examined the trafficking itinerary and molecular requirements for delivery of a model TGN protein A(F-->A)-alkaline phosphatase (ALP) to the prevacuolar/endosomal compartment (PVC). A(F-->A)-ALP was found to reach the PVC via early endosomes (EEs) with a half-time of approximately 60 min. Delivery of A(F-->A)-ALP to the PVC was not dependent on either the GGA or adaptor protein 1 (AP-1) type of clathrin adaptors, which are thought to function in TGN to PVC and TGN to EE transport, respectively. Surprisingly, in cells lacking the function of both GGA and AP-1 adaptors, A(F-->A)-ALP transport to the PVC was dramatically accelerated. A 12-residue cytosolic domain motif of A(F-->A)-ALP was found to mediate direct binding to AP-1 and was sufficient to slow TGN-->EE-->PVC trafficking. These results suggest a model in which this novel sorting signal targets A(F-->A)-ALP into clathrin/AP-1 vesicles at the EE for retrieval back to the TGN.

Indexed as

Adaptor Protein Complex 1Alkaline PhosphataseBinding SitesCell CompartmentationDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDown-RegulationEndosomesModels, BiologicalProtein BindingProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal Transductiontrans-Golgi NetworkTransport VesiclesAdaptor Protein Complex 1Alkaline PhosphataseDipeptidyl-Peptidases and Tripeptidyl-PeptidasesSaccharomyces cerevisiae ProteinsSTE13 protein, S cerevisiae

Identifiers

PMID16702232
PMCPMC2063869
OpenAlexW2077413226

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.