FEBS Journal

Cover image for Vol. 282 Issue 16

Edited By: Seamus Martin

Impact Factor: 4.001

ISI Journal Citation Reports © Ranking: 2014: 77/289 (Biochemistry & Molecular Biology)

Online ISSN: 1742-4658

Virtual Issue Reversible Tyrosine Phosphorylation Signalling and Disease


May 2010 Virtual Issue Reversible Tyrosine Phosphorylation

Papers Selected by Nicholas K. Tonks

Front cover: Figure 2 from L. Tabernero et al. (2008) FEBS J 275: 867-882.

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Introduction

This year marks the 30th anniversary of the first reports of the phosphorylation of tyrosyl residues in proteins involved in signal transduction by Tony Hunter and his colleagues [1, 2]. Developments from this groundbreaking discovery have revealed remarkable insights into the regulation of signal transduction in response to growth factors, hormones and cytokines. Furthermore, our understanding of how such signalling events are disrupted in disease has provided the foundation for new therapeutic strategies that are at the core of current approaches to treating major diseases, such as cancer. Although the focus of research was originally on the kinases, the first characterization of the protein tyrosine phosphatases (PTPs) as a novel class of signalling enzymes over 20 years ago [3, 4] helped to establish that the coordinated regulation of the activities of both protein tyrosine kinases (PTKs) and phosphatases lies at the heart of control over signal transduction. Although to a certain extent there remain kinase and phosphatase camps, such a categorization of research is somewhat artificial. Nowadays we are in the fortunate position of being able to study the fundamental importance of reversible phosphorylation, using kinases and phosphatases as complementary perspectives from which to address major problems in biology. In this Virtual Issue of FEBS Journal, I have selected some of the reviews and primary papers that have been published on this area of research in the journal since 2007. They cover various aspects of the importance of reversible tyrosine phosphorylation, and the regulation of protein tyrosine kinases and phosphatases, as well as the application of this knowledge to new approaches to therapeutic intervention. The Editorial Board of FEBS Journal encourages submission of more manuscripts in this area.

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References

1. Hunter, T. and Sefton, B.M. (1980) Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl. Acad. Sci. USA 77: 1311-1315.

2. Sefton, B.M., Hunter, T., Beemon, K. and Eckhart, W. (1980) Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. Cell 20: 807-816.

3. Tonks, N.K., Diltz, C.D. and Fischer, E.H. (1988) Purification of the major protein tyrosine phosphatases of human placenta. J. Biol. Chem. 263: 6722-6730.

4. Tonks, N.K., Diltz, C.D. and Fischer, E.H. (1988) Characterization of the major protein tyrosine phosphatases of human placenta. J. Biol. Chem. 263: 6731-6737.

Review Articles

Original Articles


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