Evidence map›Paper›PMID 28383716›Full record

ArticleNucleic acids research2017

Essential role for non-canonical poly(A) polymerase GLD4 in cytoplasmic polyadenylation and carbohydrate metabolism.

Jihae Shin, Ki Young Paek, Maria Ivshina, Emily E Stackpole, Joel D Richter

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 23% 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, 20 citations in OpenAlex.

  1. Article
  2. Measuring the tail: Methods for poly(A) tail profiling.Wiley interdisciplinary reviews. RNA · 2023
    Review
  3. The ZCCHC14/TENT4 complex is required for hepatitis A virus RNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  12. 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

5 authors at 1 institution in 1 country.

Jihae ShinProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Ki Young PaekProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Maria IvshinaProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Emily E StackpoleProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Joel D RichterProgram in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
University of Massachusetts Chan Medical School · US

Funding

POLYADENYLATION AND TRANSLATIONAL CONTROLR01GM046779 · NIGMS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI RICHTER, JOEL D · 1992 to 2022
$7.7M
Mechanisms of Translation in the CNSR01NS079415 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI RICHTER, JOEL D · 2013 to 2017
$1.9M
NIGMS NIH HHS R01 GM046779NINDS NIH HHS R01 NS079415
6 · The paper itself

Abstract

Regulation of gene expression at the level of cytoplasmic polyadenylation is important for many biological phenomena including cell cycle progression, mitochondrial respiration, and learning and memory. GLD4 is one of the non-canonical poly(A) polymerases that regulates cytoplasmic polyadenylation-induced translation, but its target mRNAs and role in cellular physiology is not well known. To assess the full panoply of mRNAs whose polyadenylation is controlled by GLD4, we performed an unbiased whole genome-wide screen using poy(U) chromatography and thermal elution. We identified hundreds of mRNAs regulated by GLD4, several of which are involved in carbohydrate metabolism including GLUT1, a major glucose transporter. Depletion of GLD4 not only reduced GLUT1 poly(A) tail length, but also GLUT1 protein. GLD4-mediated translational control of GLUT1 mRNA is dependent of an RNA binding protein, CPEB1, and its binding elements in the 3΄ UTR. Through regulating GLUT1 level, GLD4 affects glucose uptake into cells and lactate levels. Moreover, GLD4 depletion impairs glucose deprivation-induced GLUT1 up-regulation. In addition, we found that GLD4 affects glucose-dependent cellular phenotypes such as migration and invasion in glioblastoma cells. Our observations delineate a novel post-transcriptional regulatory network involving carbohydrate metabolism and glucose homeostasis mediated by GLD4.

Indexed as

Carbohydrate MetabolismPolyadenylationBase SequenceCell Line, TumorCell MovementCytoplasmGene Expression RegulationGlucose Transporter Type 1HEK293 CellsHomeostasisHumansmRNA Cleavage and Polyadenylation FactorsProtein BiosynthesisRNA, MessengerRNA NucleotidyltransferasesTranscription FactorsCPEB1 protein, humanGlucose Transporter Type 1mRNA Cleavage and Polyadenylation FactorsRNA, MessengerRNA NucleotidyltransferasesSLC2A1 protein, humanTENT4B protein, humanTranscription Factors

Identifiers

PMID28383716
PMCPMC5499868
OpenAlexW2605171817

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.