Evidence map›Paper›PMID 23046148›Full record

ArticleTraffic (Copenhagen, Denmark)2013

A sensor of protein O-glycosylation based on sequential processing in the Golgi apparatus.

Collin Bachert, Adam D Linstedt

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
0.4field-weighted citation impact, top 39% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 23 citations in OpenAlex.

  1. Pooled it
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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.

Collin BachertDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA.
Adam D Linstedt
Carnegie Mellon University · US

Funding

Fluorescent Biosensors for Networks and PathwaysU54GM103529 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WAGGONER, ALAN S. · 2012 to 2013
$6.3M
RETRIEVAL PATHWAY IN GOLGI STACK TARGETINGR01GM056779 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LINSTEDT, ADAM D · 1998 to 2015
$4.1M
STRUCTURAL BASIS OF ORGANELLE TETHERINGR01GM095549 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LINSTEDT, ADAM D · 2011 to 2014
$1.2M
NIGMS NIH HHS R01 GM056779NIGMS NIH HHS R01 GM095549NIGMS NIH HHS R01 GM56779NIGMS NIH HHS U54 GM103529
6 · The paper itself

Abstract

Protein O-glycosylation is important in numerous processes including the regulation of proteolytic processing sites by O-glycan masking in select newly synthesized proteins. To investigate O-glycan-mediated masking using an assay amenable to large-scale screens, we generated a fluorescent biosensor with an O-glycosylation site situated to mask a furin cleavage site. The sensor is activated when O-glycosylation fails to occur because furin cleavage releases a blocking domain allowing dye binding to a fluorogen activating protein. Thus, by design, glycosylation should block furin from activating the sensor only if it occurs first, which is predicted by the conventional view of Golgi organization. Indeed, and in contrast to the recently proposed rapid partitioning model, the sensor was non-fluorescent under normal conditions but became fluorescent when the Golgi complex was decompartmentalized. To test the utility of the sensor as a screening tool, cells expressing the sensor were exposed to a known inhibitor of O-glycosylation extension or siRNAs targeting factors known to alter glycosylation efficiency. These conditions activated the sensor substantiating its potential in identifying new inhibitors and cellular factors related to protein O-glycosylation. In summary, these findings confirm sequential processing in the Golgi, establish a new tool for studying the regulation of proteolytic processing by O-glycosylation, and demonstrate the sensor's potential usefulness for future screening projects.

Indexed as

Protein Processing, Post-TranslationalFurinGlycosylationGolgi ApparatusHEK293 CellsHumansMicroscopy, FluorescenceProteolysisFurin

Identifiers

PMID23046148
PMCPMC3548014
OpenAlexW1948732094

What OpenQuestion holds

Textmetadata
LicenceTDM
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.