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Sci. Signal., 15 January 2008
Vol. 1, Issue 2, p. pe2
[DOI: 10.1126/stke.12pe2]


Notch and Integrin Affinity: A Sticky Situation

Aly Karsan*

Departments of Pathology and Laboratory Medicine and Medical Biophysics, British Columbia Cancer Agency, and Department of Pathology and Laboratory Medicine, University of British Columbia, Vancouver, British Columbia V6K 2Z4, Canada.

Abstract: The Notch pathway is a conserved signal transduction system that mediates intercellular signaling to regulate cell fate decisions in various tissues. Dysregulation of Notch activity results in various disorders, including cardiovascular diseases and cancer. Notch regulates cell fate through a number of mechanisms that include control of cell proliferation, survival, migration, and differentiation. Notch activation increases vascular endothelial cell adhesion through the enhancement of β1 integrin affinity for fibronectin, collagens I and IV, and vitronectin without altering the abundance of β1 integrin at the cell surface. A study now suggests that this Notch-dependent increase in β1 integrin affinity occurs through the activation of the small guanosine triphosphate (GTP)–binding protein, R-Ras. It is proposed that Notch-dependent activation of R-Ras reverses H-Ras–mediated suppression of integrin affinity. Activation of R-Ras by Notch may be triggered by a noncanonical CSL (CBF1 or RBP-J{kappa} in vertebrates, Suppressor of Hairless in Drosophila, Lag-1 in Caenorhabditis elegans)–independent pathway. Because R-Ras is selectively distributed in vascular cells, these findings are of particular importance in understanding the effector functions of Notch in the vascular system.

*Corresponding author. E-mail, akarsan{at}

Citation: A. Karsan, Notch and Integrin Affinity: A Sticky Situation. Sci. Signal. 1, pe2 (2008).

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