Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/21590
Title: Eph receptor signalling: from catalytic to non-catalytic functions.
Authors: Liang, Lung-Yu;Patel, Onisha;Janes, Peter W;Murphy, James M;Lucet, Isabelle S
Affiliation: Department of Medical Biology, University of Melbourne, Parkville, VIC, 3052, Australia
Olivia Newton-John Cancer Research Institute, Heidelberg, Victoria, Australia
The Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia
Issue Date: 12-Aug-2019
EDate: 2019-8-12
Citation: Oncogene 2019; online first: 12 August
Abstract: Eph receptors, the largest subfamily of receptor tyrosine kinases, are linked with proliferative disease, such as cancer, as a result of their deregulated expression or mutation. Unlike other tyrosine kinases that have been clinically targeted, the development of therapeutics against Eph receptors remains at a relatively early stage. The major reason is the limited understanding on the Eph receptor regulatory mechanisms at a molecular level. The complexity in understanding Eph signalling in cells arises due to following reasons: (1) Eph receptors comprise 14 members, two of which are pseudokinases, EphA10 and EphB6, with relatively uncharacterised function; (2) activation of Eph receptors results in dimerisation, oligomerisation and formation of clustered signalling centres at the plasma membrane, which can comprise different combinations of Eph receptors, leading to diverse downstream signalling outputs; (3) the non-catalytic functions of Eph receptors have been overlooked. This review provides a structural perspective of the intricate molecular mechanisms that drive Eph receptor signalling, and investigates the contribution of intra- and inter-molecular interactions between Eph receptors intracellular domains and their major binding partners. We focus on the non-catalytic functions of Eph receptors with relevance to cancer, which are further substantiated by exploring the role of the two pseudokinase Eph receptors, EphA10 and EphB6. Throughout this review, we carefully analyse and reconcile the existing/conflicting data in the field, to allow researchers to further the current understanding of Eph receptor signalling.
URI: http://ahro.austin.org.au/austinjspui/handle/1/21590
DOI: 10.1038/s41388-019-0931-2
ORCID: 0000-0003-0195-3949
0000-0002-8563-8753
PubMed URL: 31406248
Type: Journal Article
Review
Appears in Collections:Journal articles

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