Evidence map›Paper›PMID 9693371›Full record

ArticleMolecular biology of the cell1998

Efficient trafficking of TGN38 from the endosome to the trans-Golgi network requires a free hydroxyl group at position 331 in the cytosolic domain.

E P Roquemore, G Banting

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 52 citations in OpenAlex.

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  6. Structural and functional studies of TBC1D23 C-terminal domain provide a link between endosomal trafficking and PCH.Proceedings of the National Academy of Sciences of the United States of America · 2019
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  7. Radical Stress Is More Cytotoxic in the Nucleus than in Other Organelles.International journal of molecular sciences · 2019
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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.

E P RoquemoreDepartment of Biochemistry, University of Bristol School of Medicine, University Walk, Bristol BS8 1TD, England.
G Banting
University of Bristol · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

TGN38 is one of the few known resident integral membrane proteins of the trans-Golgi network (TGN). Since it cycles constitutively between the TGN and the plasma membrane, TGN38 is ideally suited as a model protein for the identification of post-Golgi trafficking motifs. Several studies, employing chimeric constructs to detect such motifs within the cytosolic domain of TGN38, have identified the sequence 333YQRL336 as an autonomous signal capable of localizing reporter proteins to the TGN. In addition, one group has found that an upstream serine residue, S331, may also play a role in TGN38 localization. However, the nature and degree of participation of S331 in the localization of TGN38 remain uncertain, and the effect has been studied in chimeric constructs only. Here we investigate the role of S331 in the context of full-length TGN38. Mutations that abolish the hydroxyl moiety at position 331 (A, D, and E) lead to missorting of endocytosed TGN38 to the lysosome. Conversely, mutation of S331 to T has little effect on the endocytic trafficking of TGN38. Together, these findings indicate that the S331 hydroxyl group has a direct or indirect effect on the ability of the cytosolic tail of TGN38 to interact with trafficking and/or sorting machinery at the level of the early endosome. In addition, mutation of S331 to either A or D results in increased levels of TGN38 at the cell surface. The results confirm that S331 plays a critical role in the intracellular trafficking of TGN38 and further reveal that TGN38 undergoes a signal-mediated trafficking step at the level of the endosome.

Indexed as

GlycoproteinsMembrane ProteinsAmino Acid SequenceAnimalsCOS CellsCycloheximideCytosolEndocytosisEndosomesGenetic VariationGolgi ApparatusKineticsMembrane GlycoproteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedCycloheximideGlycoproteinsMembrane GlycoproteinsMembrane ProteinsPhosphatidylinositol 3-KinasesRecombinant ProteinsTgoln2 protein, rat

Identifiers

PMID9693371
PMCPMC25467
OpenAlexW2161675947

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.