Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 28 November 2000
Vol. 2000, Issue 60, p. tw4
[DOI: 10.1126/scisignal.602000tw4]

EDITORS' CHOICE

Molecular Scaffolds A Scaffold for Kinases

The β-arrestins were so named because they function in the desensitization of β2-adrenergic receptors. However, these proteins play other roles both in receptor endocytosis and in promoting receptor signaling. McDonald et al. now describe yet another function for these versatile proteins: β-arrestin 2 binds to the mitogen-activated protein kinase family member JNK3 (c-Jun NH2-terminal kinase 3) and to the upstream kinases MKK4 and ASK1 that act in a cascade to activate JNK3. β-Arrestin 2 appears to act as a scaffold that brings the kinases together and helps retain JNK3 in the cytosol. In cells treated with agonists of G protein-coupled receptors (GPCRs), the β-arrestin 2 protein appears to target JNK3 to endosomal vesicles. A perspective by Pouysségur provides greater detail on the mechanism of GPCR-mediated MAPK activation.

McDonald, P.H., Chow, C.-W., Miller, W.E., Laporte, S.A., Field, M.E., Lin, F.-T., Davis, R.J., and Lefkowitz, R.J. (2000) β-Arrestin 2: A receptor-regulated MAPK scaffold for the activation of JNK3. Science 290: 1574-1577. [Abstract] [Full Text]

Pouysségur, J. (2000) Signal Transduction: An arresting start for MAPK. Science 290: 1515-1518. [Full Text]

Citation: A Scaffold for Kinases. Sci. STKE 2000, tw4 (2000).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882