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Science 7 December 2001:
Vol. 294. no. 5549, pp. 2111 - 2113
DOI: 10.1126/science.1067628
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Perspectives

SIGNAL TRANSDUCTION:
RIPping Tyrosine Kinase Receptors Apart

Carl-Henrik Heldin and Johan Ericsson

A ligand binding to its transmembrane receptor can activate several different signaling pathways that indirectly switch on the transcription of target genes in the nucleus. As Heldin and Ericsson explain in their Perspective, new findings reveal that some receptors such as ErbB-4 can also take a more direct approach to activating gene transcription (Ni et al.). Once bound to ligand, ErbB-4 is proteolytically cleaved twice. First the ectodomain is released, then intramembrane cleavage releases a cytoplasmic fragment, which moves to the nucleus where it may affect gene expression.

The authors are at the Ludwig Institute for Cancer Research, Box 595, Biomedical Center, SE-751 24 Uppsala, Sweden.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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S.-M. Feng, C. I. Sartor, D. Hunter, H. Zhou, X. Yang, L. S. Caskey, R. Dy, R. S. Muraoka-Cook, and H. S. Earp III (2007)
Mol. Endocrinol. 21, 1861-1876
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Insulin-response Element-binding Protein 1: A NOVEL Akt SUBSTRATE INVOLVED IN TRANSCRIPTIONAL ACTION OF INSULIN.
B. C. Villafuerte, L. S. Phillips, M. J. Rane, and W. Zhao (2004)
J. Biol. Chem. 279, 36650-36659
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Alterations in the Expression of MHC Class I Glycoproteins by B16BL6 Melanoma Cells Modulate Insulin Receptor-Regulated Signal Transduction and Augments Resistance to Apoptosis.
E. Assa-Kunik, D. Fishman, S. Kellman-Pressman, S. Tsory, S. Elhyany, O. Baharir, and S. Segal (2003)
J. Immunol. 171, 2945-2952
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WW Domain-containing Protein YAP Associates with ErbB-4 and Acts as a Co-transcriptional Activator for the Carboxyl-terminal Fragment of ErbB-4 That Translocates to the Nucleus.
A. Komuro, M. Nagai, N. E. Navin, and M. Sudol (2003)
J. Biol. Chem. 278, 33334-33341
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Amyloid Precursor Protein, Presenilins, and alpha -Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer's Disease.
Y.-H. Suh and F. Checler (2002)
Pharmacol. Rev. 54, 469-525
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Science. ISSN 0036-8075 (print), 1095-9203 (online)