Evidence map›Paper›PMID 31902273›Full record

ReviewCell cycle (Georgetown, Tex.)2020

The nuclear phosphoinositide response to stress.

Mo Chen, Tianmu Wen, Hudson T Horn, Vishwanatha K Chandrahas, Narendra Thapa, Suyong Choi, Vincent L Cryns, Richard A Anderson

Open access · bronzeAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

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  19. Ribosomal targeting strategy and nuclear labeling to analyze photoreceptor phosphoinositide signatures.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2022
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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

8 authors at 1 institution in 1 country.

Mo ChenSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.
Tianmu WenSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.
Hudson T HornSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.ORCID 0000-0002-1147-4194
Vishwanatha K ChandrahasSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.
Narendra ThapaSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.
Suyong ChoiSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.
Vincent L CrynsDepartment of Medicine, University of Wisconsin Carbone Cancer Center, University of Wisconsin-Madison, School of Medicine and Public Health, Madison, WI, USA.ORCID 0000-0003-0355-2268
Richard A AndersonSchool of Medicine and Public Health, University of Wisconsin-Madison, Madison, WI, USA.
University of Wisconsin–Madison · US

Funding

Phosphoinositide Signaling in the Cytosol and NucleusR35GM134955 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Richard A. Anderson · 2020 to 2026
$5.0M
Nuclear Phosphoinositide Control of 3'-end mRNA Processing and Gene ExpressionR01GM114386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ANDERSON, RICHARD A. · 2016 to 2019
$1.5M
NIGMS NIH HHS R01 GM114386NIGMS NIH HHS R35 GM134955
6 · The paper itself

Abstract

Accumulating evidence reveals that nuclear phosphoinositides (PIs) serve as central signaling hubs that control a multitude of nuclear processes by regulating the activity of nuclear proteins. In response to cellular stressors, PIs accumulate in the nucleus and multiple PI isomers are synthesized by the actions of PI-metabolizing enzymes, kinases, phosphatases and phospholipases. By directly interacting with effector proteins, phosphoinositide signals transduce changes in cellular functions. Here we describe nuclear phosphoinositide signaling in multiple sub-nuclear compartments and summarize the literature that demonstrates roles for specific kinases, phosphatases, and phospholipases in the orchestration of nuclear phosphoinositide signaling in response to cellular stress. Additionally, we discuss the specific PI-protein complexes through which these lipids execute their functions by regulating the configuration, stability, and transcription activity of their effector proteins. Overall, our review provides a detailed landscape of the current understanding of the nuclear PI-protein interactome and its role in shaping the coordinated response to cellular stress.

Indexed as

AnimalsCell NucleusHumansNuclear ProteinsPhosphatidylinositol 3-KinasesPhosphatidylinositolsPhosphoinositide PhosphatasesSignal TransductionStress, PhysiologicalNuclear ProteinsPhosphatidylinositol 3-KinasesPhosphatidylinositolsPhosphoinositide PhosphatasesNuclear localizationphosphoinositide effectorsphosphoinositides signalingstress response

Identifiers

PMID31902273
PMCPMC7028212
OpenAlexW3000307406

What Socratic 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 Socratic graph.