Evidence map›Paper›PMID 36921042›Full record

ArticleScience advances2023

Signal recognition particle receptor-β (SR-β) coordinates cotranslational N-glycosylation.

Chatchai Phoomak, Natalie Rinis, Marta Baro, Shiteshu Shrimal, Daniel Bennett, Scott A Shaffer, Mark Lehrman, Reid Gilmore, Joseph N Contessa

Abstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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

9 authors.

Chatchai PhoomakDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, CT 06511, USA.ORCID 0000-0002-3808-8816
Natalie RinisDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, CT 06511, USA.
Marta BaroDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, CT 06511, USA.ORCID 0000-0002-6019-0534
Shiteshu ShrimalDepartment of Biochemistry and Biotechnology, University of Massachusetts Chan Medical School, Worcester, MA 01605, USA.ORCID 0000-0002-6776-5265
Daniel BennettDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, CT 06511, USA.
Scott A ShafferDepartment of Biochemistry and Biotechnology, University of Massachusetts Chan Medical School, Worcester, MA 01605, USA.ORCID 0000-0002-5264-3257
Mark LehrmanDepartment of Pharmacology, UT Southwestern Medical Center at Dallas, 6001 Forest Park Rd., Dallas, TX 75390, USA.ORCID 0000-0001-8451-0726
Reid GilmoreDepartment of Biochemistry and Biotechnology, University of Massachusetts Chan Medical School, Worcester, MA 01605, USA.ORCID 0000-0002-1656-4041
Joseph N ContessaDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, CT 06511, USA.ORCID 0000-0001-9408-1865

Funding

ASSEMBLY AND TRANSFER OF N-LINKED OLIGOSACCHARIDESR01GM043768 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GILMORE, JAMES REID · 1990 to 2018
$6.9M
The N-Glycosylation Pathway And Signaling By Free Mannose-6-PhosphateR01GM038545 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI LEHRMAN, MARK · 1987 to 2017
$5.7M
OST Inhibition in NSCLCR01CA240418 · NCI · YALE UNIVERSITY · PI CONTESSA, JOSEPH N · 2020 to 2024
$2.4M
Regulation of N-linked glycosylation in Mammalian CellsR01GM127383 · NIGMS · YALE UNIVERSITY · PI CONTESSA, JOSEPH N · 2018 to 2019
$659k
A bioluminescent screen for inhibitors of N-linked glycosylationR03DA033178 · NIDA · YALE UNIVERSITY · PI CONTESSA, JOSEPH N · 2011 to 2012
$83k
NCI NIH HHS R01 CA240418NIDA NIH HHS R03 DA033178NIGMS NIH HHS R01 GM038545NIGMS NIH HHS R01 GM043768NIGMS NIH HHS R01 GM127383
6 · The paper itself

Abstract

Proteins destined for the secretory compartment of the cell are cotranslationally translocated into the endoplasmic reticulum. The majority of these proteins are N-glycosylated, a co- and posttranslational modification that ensures proper protein folding, stability, solubility, and cellular localization. Here, we show that the [Formula: see text] subunit of the signal recognition particle receptor (SR) is required for assembly of the N-glycosylation-competent translocon. We report that guanine analog chemical probes identified by high-throughput screening or mutation of the SR-[Formula: see text] guanosine triphosphate binding site cause an N-glycosylation-deficient phenotype. Neither method alters the association of SR-[Formula: see text] with SR-[Formula: see text], but both approaches reduce the association of SR-[Formula: see text] with the oligosaccharyltransferase complex. These experiments demonstrate that SR-[Formula: see text] has a previously unrecognized function coordinating endoplasmic reticulum translation with N-glycosylation.

Indexed as

Endoplasmic ReticulumReceptors, Cytoplasmic and NuclearGlycosylationReceptors, PeptideReceptors, Cytoplasmic and NuclearReceptors, Peptidesignal peptide receptor

Identifiers

PMID36921042
PMCPMC10017033

What OpenQuestion holds

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LicenceCC BY-NC
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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.