Evidence map›Paper›PMID 16314391›Full record

ArticleMolecular biology of the cell2006

Biogenesis of tubular ER-to-Golgi transport intermediates.

Jeremy C Simpson, Tommy Nilsson, Rainer Pepperkok

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
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  9. Biological lipid nanotubes and their potential role in evolution.The European physical journal. Special topics · 2020
    Review
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  16. Glycosyltransferase-specific Golgi-targeting mechanisms.The Journal of biological chemistry · 2012
    Article
  17. Article
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  20. Contributions of electron microscopy to understand secretion of immune mediators by human eosinophils.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2010
    Review
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

3 authors at 2 institutions in 2 countries.

Jeremy C SimpsonCell Biology and Biophysics Programme, European Molecular Biology Laboratory, 69117 Heidelberg, Germany. simpson@embl.de
Tommy Nilsson
Rainer Pepperkok
European Molecular Biology Laboratory · DEUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubular transport intermediates (TTIs) have been described as one class of transport carriers in endoplasmic reticulum (ER)-to-Golgi transport. In contrast to vesicle budding and fusion, little is known about the molecular regulation of TTI synthesis, transport and fusion with target membranes. Here we have used in vivo imaging of various kinds of GFP-tagged proteins to start to address these questions. We demonstrate that under steady-state conditions TTIs represent approximately 20% of all moving transport carriers. They increase in number and length when more transport cargo becomes available at the donor membrane, which we induced by either temperature-related transport blocks or increased expression of the respective GFP-tagged transport markers. The formation and motility of TTIs is strongly dependent on the presence of intact microtubules. Microinjection of GTPgammaS increases the frequency of TTI synthesis and the length of these carriers. When Rab proteins are removed from membranes by microinjection of recombinant Rab-GDI, the synthesis of TTIs is completely blocked. Microinjection of the cytoplasmic tails of the p23 and p24 membrane proteins also abolishes formation of p24-containing TTIs. Our data suggest that TTIs are ER-to-Golgi transport intermediates that form preferentially when transport-competent cargo exists in excess at the donor membrane. We propose a model where the interaction of the cytoplasmic tails of membrane proteins with microtubules are key determinants for TTI synthesis and may also serve as a so far unappreciated model for aspects of transport carrier formation.

Indexed as

AnimalsChlorocebus aethiopsEndoplasmic ReticulumGolgi ApparatusGreen Fluorescent ProteinsHeLa CellsHumansMannose-Binding LectinsMembrane ProteinsMicrotubulesModels, BiologicalReceptors, PeptideRecombinant Fusion ProteinsTransport VesiclesVero CellsGreen Fluorescent ProteinsKDEL receptorLMAN1 protein, humanMannose-Binding LectinsMembrane ProteinsReceptors, PeptideRecombinant Fusion Proteins

Identifiers

PMID16314391
PMCPMC1356583
OpenAlexW2151613644

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.