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ERK5 : structure, regulation and function
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Nithianandarajah-Jones, Gopika N., Wilm, Bettina, Goldring, Christopher E.P., Müller, Jürgen and Cross, Michael J. (2012) ERK5 : structure, regulation and function. Cellular Signalling, Vol.24 (No.11). pp. 2187-2196. doi:10.1016/j.cellsig.2012.07.007 ISSN 0898-6568.
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Official URL: http://dx.doi.org/10.1016/j.cellsig.2012.07.007
Abstract
Extracellular signal-regulated kinase 5 (ERK5), also termed big mitogen-activated protein kinase-1 (BMK1), is the most recently identified member of the mitogen-activated protein kinase (MAPK) family and consists of an amino-terminal kinase domain, with a relatively large carboxy-terminal of unique structure and function that makes it distinct from other MAPK members. It is ubiquitously expressed in numerous tissues and is activated by a variety of extracellular stimuli, such as cellular stresses and growth factors, to regulate processes such as cell proliferation and differentiation. Targeted deletion of Erk5 in mice has revealed that the ERK5 signalling cascade plays a critical role in cardiovascular development and vascular integrity. Recent data points to a potential role in pathological conditions such as cancer and tumour angiogenesis. This review focuses on the physiological and pathological role of ERK5, the regulation of this kinase and the recent development of small molecule inhibitors of the ERK5 signalling cascade. (C) 2012 Elsevier Inc. All rights reserved.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016) Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School |
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| Journal or Publication Title: | Cellular Signalling | ||||
| Publisher: | Elsevier | ||||
| ISSN: | 0898-6568 | ||||
| Official Date: | November 2012 | ||||
| Dates: |
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| Volume: | Vol.24 | ||||
| Number: | No.11 | ||||
| Page Range: | pp. 2187-2196 | ||||
| DOI: | 10.1016/j.cellsig.2012.07.007 | ||||
| Status: | Peer Reviewed | ||||
| Publication Status: | Published | ||||
| Access rights to Published version: | Restricted or Subscription Access |
Data sourced from Thomson Reuters' Web of Knowledge
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