ERK5: structure, regulation and function

Gopika N. Nithianandarajah-Jones, Bettina Wilm, Christopher E.P. Goldring, Jürgen Müller, Michael J. Cross*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


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.

Original languageEnglish
Pages (from-to)2187-2196
Number of pages10
JournalCellular Signalling
Issue number11
Early online date12 Jul 2012
Publication statusPublished - Nov 2012


  • angiogenesis
  • big mitogen-activated protein kinase-1 (BMK1)
  • extracellular-signal-regulated kinase 5 (ERK5)
  • mitogen-activated protein kinase (MAPK)


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