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      The many substrates and functions of NEDD4-1

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          Abstract

          Tumorigenesis, tumor growth, and prognosis are highly related to gene alterations and post-translational modifications (PTMs). Ubiquitination is a critical PTM that governs practically all aspects of cellular function. An increasing number of studies show that E3 ubiquitin ligases (E3s) are important enzymes in the process of ubiquitination that primarily determine substrate specificity and thus need to be tightly controlled. Among E3s, neural precursor cell expressed developmentally downregulated 4-1 (NEDD4-1) has been shown to play a critical role in modulating the proliferation, migration, and invasion of cancer cells and the sensitivity of cancer cells to anticancer therapies via regulating multiple substrates. This review discusses some significant discoveries on NEDD4-1 substrates and the signaling pathways in which NEDD4-1 participates. In addition, we introduce the latest potential therapeutic strategies that inhibit or activate NEDD4-1 activity using small molecules. NEDD4-1 likely acts as a novel drug target or diagnostic marker in the battle against cancer.

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          Ubiquitination in disease pathogenesis and treatment.

          Doris Popovic, Domagoj Vucic, Ivan Dikic (2014)
          Ubiquitination is crucial for a plethora of physiological processes, including cell survival and differentiation and innate and adaptive immunity. In recent years, considerable progress has been made in the understanding of the molecular action of ubiquitin in signaling pathways and how alterations in the ubiquitin system lead to the development of distinct human diseases. Here we describe the role of ubiquitination in the onset and progression of cancer, metabolic syndromes, neurodegenerative diseases, autoimmunity, inflammatory disorders, infection and muscle dystrophies. Moreover, we indicate how current knowledge could be exploited for the development of new clinical therapies.
          Article 0 comments Cited 451 times – based on 0 reviews     Review now
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            LC3 conjugation system in mammalian autophagy

            Isei Tanida, Takashi Ueno, Eiki Kominami (2004)
            Autophagy is the bulk degradation of proteins and organelles, a process essential for cellular maintenance, cell viability, differentiation and development in mammals. Autophagy has significant associations with neurodegenerative diseases, cardiomyopathies, cancer, programmed cell death, and bacterial and viral infections. During autophagy, a cup-shaped structure, the preautophagosome, engulfs cytosolic components, including organelles, and closes, forming an autophagosome, which subsequently fuses with a lysosome, leading to the proteolytic degradation of internal components of the autophagosome by lysosomal lytic enzymes. During the formation of mammalian autophagosomes, two ubiquitylation-like modifications are required, Atg12-conjugation and LC3-modification. LC3 is an autophagosomal ortholog of yeast Atg8. A lipidated form of LC3, LC3-II, has been shown to be an autophagosomal marker in mammals, and has been used to study autophagy in neurodegenerative and neuromuscular diseases, tumorigenesis, and bacterial and viral infections. The other Atg8 homologues, GABARAP and GATE-16, are also modified by the same mechanism. In non-starved rats, the tissue distribution of LC3-II differs from those of the lipidated forms of GABARAP and GATE-16, GABARAP-II and GATE-16-II, suggesting that there is a functional divergence among these three modified proteins. Delipidation of LC3-II and GABARAP-II is mediated by hAtg4B. We review the molecular mechanism of LC3-modification, the crosstalk between LC3-modification and mammalian Atg12-conjugation, and the cycle of LC3-lipidation and delipidation mediated by hAtg4B, as well as recent findings concerning the other two Atg8 homologues, GABARAP and GATE-16. We also highlight recent findings regarding the pathobiology of LC3-modification, including its role in microbial infection, cancer and neuromuscular diseases.
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              Novel anticancer targets: revisiting ERBB2 and discovering ERBB3.

              José Baselga, Sandra M Swain (2009)
              Aberrant receptor expression or functioning of the epidermal growth factor receptor (Erbb) family plays a crucial part in the development and evolution of cancer. Inhibiting the signalling activity of individual receptors in this family has advanced the treatment of a range of human cancers. In this Review we re-evaluate the role of two important family members, ERBB2 (also known as HER2) and ERBB3 (also known as HER3), and explore the mechanisms of action and preclinical and clinical data for new therapies that target signalling through these pivotal receptors. These new therapies include tyrosine kinase inhibitors, antibody-chemotherapy conjugates, heat-shock protein inhibitors and antibodies that interfere with the formation of ERBB2-ERBB3 dimers.
              Article 0 comments Cited 364 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Enfan Zhang: +0086-571-87236706 , efzhang@zju.edu.cn
                Zhen Cai:
                ORCID: http://orcid.org/0000-0002-6327-5066
                +0086-571-87236706 , caiz@zju.edu.cn
                Journal
                Journal ID (nlm-ta): Cell Death Dis
                Journal ID (iso-abbrev): Cell Death Dis
                Title: Cell Death & Disease
                Publisher: Nature Publishing Group UK (London )
                ISSN (Electronic): 2041-4889
                Publication date (Electronic): 2 December 2019
                Publication date PMC-release: 2 December 2019
                Publication date Collection: December 2019
                Volume: 10
                Issue: 12
                Electronic Location Identifier: 904
                Affiliations
                [1 ]ISNI 0000 0004 1759 700X, GRID grid.13402.34, Bone Marrow Transplantation Center, Department of Hematology, The First Affiliated Hospital, School of Medicine, , Zhejiang University, ; Hangzhou, China
                [2 ]ISNI 0000 0004 0445 0041, GRID grid.63368.38, Center for Hematologic Malignancy Research Institute, , Houston Methodist, ; Houston, TX USA
                [3 ]ISNI 0000 0004 1759 700X, GRID grid.13402.34, Institute of Hematology, , Zhejiang University, ; Hangzhou, China
                Author information
                http://orcid.org/0000-0002-6327-5066
                Article
                Publisher ID: 2142
                DOI: 10.1038/s41419-019-2142-8
                PMC ID: 6885513
                PubMed ID: 31787758
                SO-VID: 0f875b58-cd0c-4548-a097-6da895afcb78
                Copyright © © The Author(s) 2019
                License:

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                Date received : 21 August 2019
                Date revision received : 24 October 2019
                Date accepted : 12 November 2019
                Funding
                Funded by: FundRef https://doi.org/10.13039/501100001809, National Natural Science Foundation of China (National Science Foundation of China);
                Award ID: 91742110
                Award ID: 81872322
                Award Recipient :
                Categories
                Subject: Review Article
                Custom metadata
                issue-copyright-statement © The Author(s) 2019

                ScienceOpen disciplines: Cell biology
                Keywords: tumour biomarkers,ubiquitylation
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: tumour biomarkers, ubiquitylation

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