Evidence map›Paper›PMID 27002730›Full record

ReviewThe AAPS journal2016

RGS6 as a Novel Therapeutic Target in CNS Diseases and Cancer.

Katelin E Ahlers, Bandana Chakravarti, Rory A Fisher

Abstract readReview
In one paragraph

Review in The AAPS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

32 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. SMARCA4 Loss and Mutated β-Catenin Induce Proliferative Lesions in the Murine Embryonic Cerebellum.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Novel Molecular Targets of Antidepressants.Molecules (Basel, Switzerland) · 2022
    Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Katelin E AhlersDepartment of Pharmacology, The Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 2-505 Bowen Science Building, Iowa City, Iowa, 52242, USA.
Bandana ChakravartiDepartment of Pharmacology, The Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 2-505 Bowen Science Building, Iowa City, Iowa, 52242, USA.
Rory A FisherDepartment of Pharmacology, The Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 2-505 Bowen Science Building, Iowa City, Iowa, 52242, USA. rory-fisher@uiowa.edu.ORCID 0000-0003-3108-4836
University of Iowa · US

Funding

Molecular Analysis and Role of RGS6 as a Novel Growth SuppressorR01CA161882 · NCI · UNIVERSITY OF IOWA · PI FISHER, RORY A. · 2012 to 2016
$1.5M
NCI NIH HHS CA161882NCI NIH HHS R01 CA161882
6 · The paper itself

Abstract

Regulator of G protein signaling (RGS) proteins are gatekeepers regulating the cellular responses induced by G protein-coupled receptor (GPCR)-mediated activation of heterotrimeric G proteins. Specifically, RGS proteins determine the magnitude and duration of GPCR signaling by acting as a GTPase-activating protein for Gα subunits, an activity facilitated by their semiconserved RGS domain. The R7 subfamily of RGS proteins is distinguished by two unique domains, DEP/DHEX and GGL, which mediate membrane targeting and stability of these proteins. RGS6, a member of the R7 subfamily, has been shown to specifically modulate Gαi/o protein activity which is critically important in the central nervous system (CNS) for neuronal responses to a wide array of neurotransmitters. As such, RGS6 has been implicated in several CNS pathologies associated with altered neurotransmission, including the following: alcoholism, anxiety/depression, and Parkinson's disease. In addition, unlike other members of the R7 subfamily, RGS6 has been shown to regulate G protein-independent signaling mechanisms which appear to promote both apoptotic and growth-suppressive pathways that are important in its tumor suppressor function in breast and possibly other tissues. Further highlighting the importance of RGS6 as a target in cancer, RGS6 mediates the chemotherapeutic actions of doxorubicin and blocks reticular activating system (Ras)-induced cellular transformation by promoting degradation of DNA (cytosine-5)-methyltransferase 1 (DNMT1) to prevent its silencing of pro-apoptotic and tumor suppressor genes. Together, these findings demonstrate the critical role of RGS6 in regulating both G protein-dependent CNS pathology and G protein-independent cancer pathology implicating RGS6 as a novel therapeutic target.

Indexed as

AnimalsAntineoplastic AgentsCell Transformation, NeoplasticCentral Nervous System DiseasesDrug Delivery SystemsHumansNeoplasmsReceptors, G-Protein-CoupledRGS ProteinsSignal TransductionAntineoplastic AgentsReceptors, G-Protein-CoupledRGS6 protein, humanRGS ProteinsalcoholismdepressiondoxorubicinParkinson’s diseaseRGS protein

Identifiers

PMID27002730
PMCPMC5256616
OpenAlexW2306119948

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.