Evidence map›Paper›PMID 33822486›Full record

ReviewCancer reports (Hoboken, N.J.)2021

The FBXW7-NOTCH interactome: A ubiquitin proteasomal system-induced crosstalk modulating oncogenic transformation in human tissues.

Rohan Kar, Saurabh Kumar Jha, Shreesh Ojha, Ankur Sharma, Sunny Dholpuria, Venkata Sita Rama Raju, Parteek Prasher, Dinesh Kumar Chellappan, Gaurav Gupta, Sachin Kumar Singh and 7 more

Open access · goldAbstract readReview
In one paragraph

Review in Cancer reports (Hoboken, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 26 citations in OpenAlex.

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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

17 authors at 10 institutions in 6 countries.

Rohan KarIndian Institute of Management Ahmedabad (IIMA), Ahmedabad, Gujarat, 380015, India.ORCID 0000-0002-7903-4558
Saurabh Kumar JhaDepartment of Biotechnology, School of Engineering & Technology (SET), Sharda University, Greater Noida, Uttar Pradesh, 201310, India.ORCID 0000-0002-7437-0755
Shreesh OjhaDepartment of Pharmacology and Therapeutics, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, 17666, United Arab Emirates.ORCID 0000-0001-7801-2966
Ankur SharmaDepartment of Life sciences, School of Basic Science & Research (SBSR), Sharda University, Greater Noida, Uttar Pradesh, 201310, India.ORCID 0000-0003-3058-760X
Sunny DholpuriaDepartment of Life sciences, School of Basic Science & Research (SBSR), Sharda University, Greater Noida, Uttar Pradesh, 201310, India.
Venkata Sita Rama RajuDepartment of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.
Parteek PrasherDepartment of Chemistry, University of Petroleum & Energy Studies, Dehradun, 248007, India.
Dinesh Kumar ChellappanDepartment of Life Sciences, School of Pharmacy, International Medical University (IMU), Bukit Jalil, Kuala Lumpur, 57000, Malaysia.
Gaurav GuptaSchool of Pharmacy, Suresh Gyan Vihar University, Jagatpura, Jaipur, 302017, India.
Sachin Kumar SinghSchool of Pharmaceutical Sciences, Lovely Professional University, Phagwara, Punjab, 144411, India.
Keshav Raj PaudelCentre for Inflammation, Centenary Institute, New South Wales, 2050, Australia.
Philip M HansbroCentre for Inflammation, Centenary Institute, New South Wales, 2050, Australia.
Sandeep Kumar SinghIndian Scientific Education and Technology Foundation, Lucknow, Uttar Pradesh, 226002, India.
Janne RuokolainenDepartment of Applied Physics, School of Science, Aalto University, Espoo, Finland.
Kavindra Kumar KesariDepartment of Applied Physics, School of Science, Aalto University, Espoo, Finland.ORCID 0000-0003-3622-9555
Kamal DuaCentre for Inflammation, Centenary Institute, New South Wales, 2050, Australia.ORCID 0000-0002-7507-1159
Niraj Kumar JhaDepartment of Biotechnology, School of Engineering & Technology (SET), Sharda University, Greater Noida, Uttar Pradesh, 201310, India.ORCID 0000-0001-9486-4069
Sharda University · INUniversity of Technology Sydney · AUAalto University · FILovely Professional University · INGyan Vihar University · INIMU University · MYIndian Institute of Management Ahmedabad · INUnited Arab Emirates University · AEUniversity of Petroleum and Energy Studies · INUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundUbiquitin ligases or E3 ligases are well programmed to regulate molecular interactions that operate at a post-translational level. Skp, Cullin, F-box containing complex (or SCF complex) is a multidomain E3 ligase known to mediate the degradation of a wide range of proteins through the proteasomal pathway. The three-dimensional domain architecture of SCF family proteins suggests that it operates through a novel and adaptable "super-enzymatic" process that might respond to targeted therapeutic modalities in cancer. RECENT

findingsSeveral F-box containing proteins have been characterized either as tumor suppressors (FBXW8, FBXL3, FBXW8, FBXL3, FBXO1, FBXO4, and FBXO18) or as oncogenes (FBXO5, FBXO9, and SKP2). Besides, F-box members like βTrcP1 and βTrcP2, the ones with context-dependent functionality, have also been studied and reported. FBXW7 is a well-studied F-box protein and is a tumor suppressor. FBXW7 regulates the activity of a range of substrates, such as c-Myc, cyclin E, mTOR, c-Jun, NOTCH, myeloid cell leukemia sequence-1 (MCL1), AURKA, NOTCH through the well-known ubiquitin-proteasome system (UPS)-mediated degradation pathway. NOTCH signaling is a primitive pathway that plays a crucial role in maintaining normal tissue homeostasis. FBXW7 regulates NOTCH protein activity by controlling its half-life, thereby maintaining optimum protein levels in tissue. However, aberrations in the FBXW7 or NOTCH expression levels can lead to poor prognosis and detrimental outcomes in patients. Therefore, the FBXW7-NOTCH axis has been a subject of intense study and research over the years, especially around the interactome's role in driving cancer development and progression. Several studies have reported the effect of FBXW7 and NOTCH mutations on normal tissue behavior. The current review attempts to critically analyze these mutations prognostic value in a wide range of tumors. Furthermore, the review summarizes the recent findings pertaining to the FBXW7 and NOTCH interactome and its involvement in phosphorylation-related events, cell cycle, proliferation, apoptosis, and metastasis.

conclusionThe review concludes by positioning FBXW7 as an effective diagnostic marker in tumors and by listing out recent advancements made in cancer therapeutics in identifying protocols targeting the FBXW7-NOTCH aberrations in tumors.

Indexed as

AnimalsCell Transformation, NeoplasticDisease Models, AnimalF-Box-WD Repeat-Containing Protein 7Gene Expression Regulation, NeoplasticHumansMutationNeoplasmsPhosphorylationPrognosisProteasome Endopeptidase ComplexProtein Interaction MapsProteolysisReceptors, NotchUbiquitinF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanProteasome Endopeptidase ComplexReceptors, NotchUbiquitincancerdiagnostic markersE3 ligaseFBXW7mutationNOTCHSCFtherapeutics

Identifiers

PMID33822486
PMCPMC8388169
OpenAlexW3152076948

What Socratic holds

Textmetadata
LicenceCC BY
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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 Socratic graph.