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Sci. Signal., 25 October 2011
Vol. 4, Issue 196, p. re3
[DOI: 10.1126/scisignal.2002324]

REVIEWS

Working Without Kinase Activity: Phosphotransfer-Independent Functions of Extracellular Signal–Regulated Kinases

Javier Rodríguez and Piero Crespo*

Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Consejo Superior de Investigaciones Científicas (CSIC)—IDICAN—Universidad de Cantabria. Departamento de Biología Molecular, Facultad de Medicina. Santander, 39011, Cantabria, Spain.

Gloss: Extracellular signal–regulated kinase 1 (ERK1) and ERK2 are typical serine and threonine kinases that are members of the family of mitogen-activated protein kinases and are involved in the regulation of key cellular processes, including proliferation, differentiation, and survival, through the phosphorylation of nearly 200 substrates. However, accumulating evidence demonstrates that ERK1 and ERK2 can also function independently of their kinase activities in the control of critical biochemical and biological events, such as chromatin remodeling, DNA transcription, and cell cycle regulation. In this Review, which contains 1 figure and 72 references, we summarize findings from a number of studies that underline the importance of these kinase-independent roles of the ERKs.

*Corresponding author. E-mail: crespop{at}unican.es

Citation: J. Rodríguez, P. Crespo, Working Without Kinase Activity: Phosphotransfer-Independent Functions of Extracellular Signal–Regulated Kinases. Sci. Signal. 4, re3 (2011).


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