Evidence map›Paper›PMID 18564369›Full record

ArticleTraffic (Copenhagen, Denmark)2008

In situ cleavage of the acidic domain from the p115 tether inhibits exocytic transport.

Ayano Satoh, Graham Warren

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  6. The golgin coiled-coil proteins of the Golgi apparatus.Cold Spring Harbor perspectives in biology · 2011
    Review
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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 2 countries.

Ayano SatohDepartment of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520-8002, USA.
Graham Warren
Yale University · US

Funding

MEMBRANE FUSION ATPASES AND THE GOLGI APPARATUSR01GM060919 · NIGMS · YALE UNIVERSITY · PI SATOH, AYANO · 2000 to 2007
$2.5M
The role of phosphorylation of a COPII coat protein, Sec31 in molecular exportR03AG030101 · NIA · YALE UNIVERSITY · PI DE CAMILLI, PIETRO · 2008 to 2009
$136k
NIA NIH HHS AG030101NIA NIH HHS R03 AG030101NIGMS NIH HHS GM060919NIGMS NIH HHS R01 GM060919
6 · The paper itself

Abstract

Golgins are coiled-coil proteins involved in Golgi architecture and function. A complex of golgins (p115, GM130 and giantin), together with the rab1 guanosine triphosphatase and cis Golgi SNAREs, helps to mediate fusion processes at the entry face of the Golgi apparatus. The C-terminal acidic domain of p115 binds specifically to GM130 and giantin. However, deletion of this domain in vivo appears to have no effect on exocytic transport when using an RNA interference depletion/rescue approach (Puthenveedu MA, Linstedt AD. Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis. Proc Natl Acad Sci U S A 2004;101:1253-1256). In this study, we have used a different approach introducing a tobacco etch virus (tev) protease cleavage site into p115 so that the C-terminal domain can be rapidly and specifically released in vivo by microinjection of the tev protease. The results show that cleavage inhibits exocytic transport to the cell surface.

Indexed as

ExocytosisMembrane FusionAutoantigensBinding SitesBlotting, WesternCoat Protein Complex IEndopeptidasesGolgi ApparatusGolgi Matrix ProteinsHeLa CellsHumansImmunoprecipitationMembrane ProteinsMicroscopy, FluorescencePeptide FragmentsProtein BindingAutoantigensCoat Protein Complex IEndopeptidasesGolgi Matrix ProteinsGolgin subfamily A member 2macrogolginMembrane ProteinsPeptide FragmentsTEV proteasevesicular transport factor p115Vesicular Transport Proteins

Identifiers

PMID18564369
PMCPMC3035718
OpenAlexW2062460908

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.