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Sci. STKE, 25 April 2000
Vol. 2000, Issue 29, p. pe1
[DOI: 10.1126/stke.2000.29.pe1]

RIPping Notch Apart: A New Role for Endocytosis in Signal Transduction?

Helmut Krämer

The author is at the Center for Basic Neuroscience and Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75235-9111, USA. E-mail: kramer{at}utsw.swmed.edu

Abstract: Notch proteins are receptors that are important in mediating several developmental processes. Notch receptors are activated upon binding transmembrane ligands, the DSL proteins. Notch is cleaved at several sites and activation of Notch leads to the cleavage of the intracellular domain, which then is translocated to the nucleus and regulates the transcription of target genes. Krämer discusses how binding of Notch to the DSL ligand, Delta, leads to cleavage and trans-endocytosis of the Notch extracellular domain into the Delta-expressing cell. This trans-endocytosis event contributes to the cleavage and release of the active Notch intracellular domain. The Perspective is accompanied by a movie illustrating the trans-endocytosis of Notch.

Citation: H. Krämer, RIPping Notch Apart: A New Role for Endocytosis in Signal Transduction? Sci. STKE 2000, pe1 (2000).

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