Evidence map›Paper›PMID 29026529›Full record

ReviewF1000Research2017

Coordinating ERK signaling via the molecular scaffold Kinase Suppressor of Ras.

Danielle Frodyma, Beth Neilsen, Diane Costanzo-Garvey, Kurt Fisher, Robert Lewis

Open access · goldAbstract readReview
In one paragraph

Review in F1000Research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  19. Genetics of Severe Obesity.Current diabetes reports · 2018
    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.

Danielle FrodymaEppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA.
Beth NeilsenEppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA.
Diane Costanzo-GarveyEppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA.
Kurt FisherDepartment of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska, USA.
Robert LewisEppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska, USA.ORCID https://orcid.org/0000-0002-3616-2971
University of Nebraska Medical Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Apar Kishor Ganti · 1985 to 2026
$55.0M
The role of stress in the fetal origin of obesity and metabolic dysfunctionP20GM104320 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2014 to 2024
$24.9M
CHEMICAL CARCINOGENESIS &CANCER BIOLOGYT32CA009476 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Jennifer D. Black · 1988 to 2026
$6.2M
Novel Effectors of Colon TumorigenesisR01CA157774 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LEWIS, ROBERT E. · 2012 to 2016
$1.5M
Discovering Vulnerabilities in Ras-driven CancersF30CA203397 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI NEILSEN, BETH · 2016 to 2019
$165k
NCI NIH HHS F30 CA203397NCI NIH HHS P30 CA036727NCI NIH HHS R01 CA157774NCI NIH HHS T32 CA009476NIGMS NIH HHS P20 GM104320
6 · The paper itself

Abstract

Many cancers, including those of the colon, lung, and pancreas, depend upon the signaling pathways induced by mutated and constitutively active Ras. The molecular scaffolds Kinase Suppressor of Ras 1 and 2 (KSR1 and KSR2) play potent roles in promoting Ras-mediated signaling through the Raf/MEK/ERK kinase cascade. Here we summarize the canonical role of KSR in cells, including its central role as a scaffold protein for the Raf/MEK/ERK kinase cascade, its regulation of various cellular pathways mediated through different binding partners, and the phenotypic consequences of KSR1 or KSR2 genetic inactivation. Mammalian KSR proteins have a demonstrated role in cellular and organismal energy balance with implications for cancer and obesity. Targeting KSR1 in cancer using small molecule inhibitors has potential for therapy with reduced toxicity to the patient. RNAi and small molecule screens using KSR1 as a reference standard have the potential to expose and target vulnerabilities in cancer. Interestingly, although KSR1 and KSR2 are similar in structure, KSR2 has a distinct physiological role in regulating energy balance. Although KSR proteins have been studied for two decades, additional analysis is required to elucidate both the regulation of these molecular scaffolds and their potent effect on the spatial and temporal control of ERK activation in health and disease.

Indexed as

ERK SignallingKinase Suppressor of RasKSR

Identifiers

PMID29026529
PMCPMC5583734
OpenAlexW2753075117

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.