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

First Author  Schulz JG Year  2003
Journal  J Biol Chem Volume  278
Issue  49 Pages  48651-7
PubMed ID  14504279 Mgi Jnum  J:86802
Mgi Id  MGI:2682114 Doi  10.1074/jbc.M308424200
Citation  Schulz JG, et al. (2003) Syndecan 3 intramembrane proteolysis is presenilin/gamma-secretase-dependent and modulates cytosolic signaling. J Biol Chem 278(49):48651-7
abstractText  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 which are required for signaling across the membrane and for interaction with cytosolic proteins. However, regulatory mechanisms controlling these functions remain 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/gamma-secretase complex and negatively regulates the plasma membrane targeting of the transcriptional cofactor CASK.
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