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A more recent version of this article appeared on December 5, 2003 Originally published In Press as doi:10.1074/jbc.M308424200 on September 22, 2003
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Papers In Press, published online ahead of print September 26, 2003
J. Biol. Chem, 10.1074/jbc.M308424200
Submitted on July 31, 2003
Revised on September 17, 2003
Accepted on September 22, 2003

Syndecan 3 intramembrane proteolysis is presenilin/gamma -secretase-dependent and modulates cytosolic signaling

Joachim G Schulz, Wim Annaert, Joël Vandekerckhove, Pascale Zimmermann, Bart De Strooper, and Guido David

Department of Human Genetics, University of Leuven, Leuven B-3000

Corresponding Author: guido.david{at}med.kuleuven.ac.be

The syndecans play critical roles in several signal transduction pathways. The core proteins of these heparan sulfate proteoglycans are characterized by highly conserved transmembrane and intracellular domains, required for signaling across the membrane and for interaction with cytosolic proteins. Regulatory mechanisms controlling these functions remain, however, largely unknown. Here we show that, upon ligand-induced primary proteolytic cleavage within the ectodomain, the intracellular domain of syndecan 3 is released by regulated intramembrane proteolysis. The cleavage is mediated by presenilin/g-secretase complex and negatively regulates the plasma membrane targeting of the transcriptional cofactor CASK.


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