A review on cullin neddylation and strategies to identify its inhibitors for cancer therapy.

Cancer Cullin-RING E3 ligase Inhibitor NEDD8 Neddylation

Journal

3 Biotech
ISSN: 2190-572X
Titre abrégé: 3 Biotech
Pays: Germany
ID NLM: 101565857

Informations de publication

Date de publication:
Apr 2022
Historique:
received: 06 10 2021
accepted: 29 01 2022
entrez: 25 4 2022
pubmed: 26 4 2022
medline: 26 4 2022
Statut: ppublish

Résumé

The cullin-RING E3 ligases (CRLs) are the biggest components of the E3 ubiquitin ligase protein family, and they represent an essential role in various diseases that occur because of abnormal activation, particularly in tumors development. Regulation of CRLs needs neddylation, a post-translational modification involving an enzymatic cascade that transfers small, ubiquitin-like NEDD8 protein to CRLs. Many previous studies have confirmed neddylation as an enticing target for anticancer drug discoveries, and few recent studies have also found a significant increase in advancement in protein neddylation, including preclinical and clinical target validation to discover the neddylation inhibitor compound. In the present review, we first presented briefly the essence of CRLs' neddylation and its control, systematic analysis of CRLs, followed by the description of a few recorded chemical inhibitors of CRLs neddylation enzymes with recent examples of preclinical and clinical targets. We have also listed various structure-based pointing of protein-protein dealings in the CRLs' neddylation reaction, and last, the methods available to discover new inhibitors of neddylation are elaborated. This review will offer a concentrated, up-to-date, and detailed description of the discovery of neddylation inhibitors.

Identifiants

pubmed: 35463041
doi: 10.1007/s13205-022-03162-x
pii: 3162
pmc: PMC8964847
doi:

Types de publication

Journal Article

Langues

eng

Pagination

103

Informations de copyright

© King Abdulaziz City for Science and Technology 2022.

Déclaration de conflit d'intérêts

Conflict of interestThe authors declare no conflict of interest could be perceived as prejudicial to the impartiality of the reported research.

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Auteurs

Iqra Bano (I)

Department of Veterinary Physiology and Biochemistry, Shaheed Benazir Bhutto University of Veterinary and Animals Sciences Sakrand (SBBUVAS), Sakrand, 67210 Sindh Pakistan.

Moolchand Malhi (M)

Faculty of Animal Husbandry and Veterinary Sciences, Sindh Agriculture University, Tandojam, Pakistan.

Min Zhao (M)

Collaborative Innovation Center of New Drug Research and Safety Evaluation, Henan Province, and Key Laboratory of Advanced Drug Preparation Technologies, School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001 Henan People's Republic of China.

Liviu Giurgiulescu (L)

Chemistry-Biology Department, Technical University of Cluj Napoca, North University Center of Baia Mare, 26 Victoriei St., Baia Mare, Romania.

Hira Sajjad (H)

Faculty of Animal Husbandry and Veterinary Sciences, Sindh Agriculture University, Tandojam, Pakistan.

Marek Kieliszek (M)

Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159 C, 02-776 Warsaw, Poland.

Classifications MeSH