Evidence map›Paper›PMID 19457257›Full record

ArticleBMC biotechnology2009

Peroxicretion: a novel secretion pathway in the eukaryotic cell.

Cees M J Sagt, Peter J ten Haaft, Ingeborg M Minneboo, Miranda P Hartog, Robbert A Damveld, Jan Metske van der Laan, Michiel Akeroyd, Thibaut J Wenzel, Francisca A Luesken, Marten Veenhuis and 2 more

Abstract read
In one paragraph

Article in BMC biotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Review
  2. Article
  3. Destructuring plant biomass: focus on fungal and extremophilic cell wall hydrolases.Plant science : an international journal of experimental plant biology · 2015
    Review
  4. Article
  5. Review
  6. 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

12 authors.

Cees M J SagtDSM Biotechnology Center, Beijerinck Laboratory, PO Box 1, 2600MA Delft, the Netherlands. cees.sagt@dsm.com
Peter J ten Haaft
Ingeborg M Minneboo
Miranda P Hartog
Robbert A Damveld
Jan Metske van der Laan
Michiel Akeroyd
Thibaut J Wenzel
Francisca A Luesken
Marten Veenhuis
Ida van der Klei
Johannes H de Winde

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEnzyme production in microbial cells has been limited to secreted enzymes or intracellular enzymes followed by expensive down stream processing. Extracellular enzymes consists mainly of hydrolases while intracellular enzymes exhibit a much broader diversity. If these intracellular enzymes could be secreted by the cell the potential of industrial applications of enzymes would be enlarged. Therefore a novel secretion pathway for intracellular proteins was developed, using peroxisomes as secretion vesicles.

resultsPeroxisomes were decorated with a Golgi derived v-SNARE using a peroxisomal membrane protein as an anchor. This allowed the peroxisomes to fuse with the plasma membrane. Intracellular proteins were transported into the peroxisomes by adding a peroxisomal import signal (SKL tag). The proteins which were imported in the peroxisomes, were released into the extra-cellular space through this artificial secretion pathway which was designated peroxicretion. This concept was supported by electron microscopy studies.

conclusionOur results demonstrate that it is possible to reroute the intracellular trafficking of vesicles by changing the localisation of SNARE molecules, this approach can be used in in vivo biological studies to clarify the different control mechanisms regulating intracellular membrane trafficking. In addition we demonstrate peroxicretion of a diverse set of intracellular proteins. Therefore, we anticipate that the concept of peroxicretion may revolutionize the production of intracellular proteins from fungi and other microbial cells, as well as from mammalian cells.

Indexed as

Secretory PathwayAspergillus nigerCell MembraneGreen Fluorescent ProteinsMembrane ProteinsPeroxisomesPeroxisome-Targeting Signal 1 ReceptorProtein TransportReceptors, Cytoplasmic and NuclearSNARE Proteinsenhanced green fluorescent proteinGreen Fluorescent ProteinsMembrane ProteinsPeroxisome-Targeting Signal 1 ReceptorReceptors, Cytoplasmic and NuclearSNARE Proteins

Identifiers

PMID19457257
PMCPMC2693430

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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.