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      Emerging Roles for Eph Receptors and Ephrin Ligands in Immunity

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          Abstract

          Eph receptors are the largest family of receptor tyrosine kinases and mediate a myriad of essential processes in humans from embryonic development to adult tissue homeostasis through interactions with membrane-bound ephrin ligands. The ubiquitous expression of Eph receptors and ephrin ligands among the cellular players of the immune system underscores the importance of these molecules in orchestrating an optimal immune response. This review provides an overview of the various roles of Eph receptors and ephrin ligands in immune cell development, activation, and migration. We also discuss the role of Eph receptors in disease pathogenesis as well as the implications of Eph receptors as future immunotherapy targets. Given the diverse and critical roles of Eph receptors and ephrin ligands throughout the immune system during both resting and activated states, this review aims to highlight the critical yet underappreciated roles of this family of signaling molecules in the immune system.

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          Most cited references144

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          The protein kinase complement of the human genome.

          G. Manning (2002)
          We have catalogued the protein kinase complement of the human genome (the "kinome") using public and proprietary genomic, complementary DNA, and expressed sequence tag (EST) sequences. This provides a starting point for comprehensive analysis of protein phosphorylation in normal and disease states, as well as a detailed view of the current state of human genome analysis through a focus on one large gene family. We identify 518 putative protein kinase genes, of which 71 have not previously been reported or described as kinases, and we extend or correct the protein sequences of 56 more kinases. New genes include members of well-studied families as well as previously unidentified families, some of which are conserved in model organisms. Classification and comparison with model organism kinomes identified orthologous groups and highlighted expansions specific to human and other lineages. We also identified 106 protein kinase pseudogenes. Chromosomal mapping revealed several small clusters of kinase genes and revealed that 244 kinases map to disease loci or cancer amplicons.
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            Eph receptor signalling casts a wide net on cell behaviour.

            Elena B. Pasquale (2005)
            Eph receptor tyrosine kinases mould the behaviour of many cell types by binding membrane-anchored ligands, ephrins, at sites of cell-cell contact. Eph signals affect both of the contacting cells and can produce diverse biological responses. New models explain how quantitative variations in the densities and signalling abilities of Eph receptors and ephrins could account for the different effects that are elicited on axon guidance, cell adhesion and cell migration during development, homeostasis and disease.
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              Small extracellular vesicles secreted from senescent cells promote cancer cell proliferation through EphA2

              Masaki Takasugi, Ryo Okada, Akiko Takahashi … (2017)
              Cellular senescence prevents the proliferation of cells at risk for neoplastic transformation. However, the altered secretome of senescent cells can promote the growth of the surrounding cancer cells. Although extracellular vesicles (EVs) have emerged as new players in intercellular communication, their role in the function of senescent cell secretome has been largely unexplored. Here, we show that exosome-like small EVs (sEVs) are important mediators of the pro-tumorigenic function of senescent cells. sEV-associated EphA2 secreted from senescent cells binds to ephrin-A1, that is, highly expressed in several types of cancer cells and promotes cell proliferation through EphA2/ephrin-A1 reverse signalling. sEV sorting of EphA2 is increased in senescent cells because of its enhanced phosphorylation resulting from oxidative inactivation of PTP1B phosphatase. Our results demonstrate a novel mechanism of reactive oxygen species (ROS)-regulated cargo sorting into sEVs, which is critical for the potentially deleterious growth-promoting effect of the senescent cell secretome.
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                Author and article information

                Contributors
                Journal
                Journal ID (nlm-ta): Front Immunol
                Journal ID (iso-abbrev): Front Immunol
                Journal ID (publisher-id): Front. Immunol.
                Title: Frontiers in Immunology
                Publisher: Frontiers Media S.A.
                ISSN (Electronic): 1664-3224
                Publication date (Electronic): 04 July 2019
                Publication date Collection: 2019
                Volume: 10
                Electronic Location Identifier: 1473
                Affiliations
                [1] 1Immunology and Molecular Pathogenesis Program, Emory University Laney Graduate School , Atlanta, GA, United States
                [2] 2Department of Pathology, University of Utah , Salt Lake City, UT, United States
                Author notes

                Edited by: Moncef Zouali, Institut National de la Santé et de la Recherche Médicale (INSERM), France

                Reviewed by: Peter Warwick Janes, Monash University, Australia; Marit Inngjerdingen, Oslo University Hospital, Norway

                *Correspondence: Tracey J. Lamb tracey.lamb@ 123456path.utah.edu

                This article was submitted to Molecular Innate Immunity, a section of the journal Frontiers in Immunology

                Article
                DOI: 10.3389/fimmu.2019.01473
                PMC ID: 6620610
                PubMed ID: 31333644
                SO-VID: 271de596-73ce-4533-bdc7-f23fd4bf95f3
                Copyright © Copyright © 2019 Darling and Lamb.
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                Date received : 13 March 2019
                Date accepted : 13 June 2019
                Page count
                Figures: 2, Tables: 2, Equations: 0, References: 177, Pages: 15, Words: 12650
                Funding
                Funded by: National Institutes of Health 10.13039/100000002
                Categories
                Subject: Immunology
                Subject: Review

                ScienceOpen disciplines: Immunology
                Keywords: eph,ephrin,activation,cell trafficking,migration,adhesion,inflammation,disease
                Data availability:
                ScienceOpen disciplines: Immunology
                Keywords: eph, ephrin, activation, cell trafficking, migration, adhesion, inflammation, disease

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