Ligand-induced dimerization of syndecan-3 at the cell surface

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Kulesskiy , E , Tumova , S & Rauvala , H 2013 , ' Ligand-induced dimerization of syndecan-3 at the cell surface ' , Advances in Bioscience and Biotechnology , vol. 4 , no. 6A , pp. 36-44 . https://doi.org/10.4236/abb.2013.46A006

Title: Ligand-induced dimerization of syndecan-3 at the cell surface
Author: Kulesskiy, Evgeny; Tumova, Sarka; Rauvala, Heikki
Contributor: University of Helsinki, Neuroscience Center
University of Helsinki, Neuroscience Center
Date: 2013-06-20
Language: eng
Number of pages: 9
Belongs to series: Advances in Bioscience and Biotechnology
ISSN: 2156-8456
URI: http://hdl.handle.net/10138/162218
Abstract: Syndecan-3 (N-syndecan) is a transmembrane heparan sulfate proteoglycan abundantly expressed in developing brain. In addition to acting as a coreceptor, syndecan-3 acts as a signaling receptor upon binding of its ligand HB-GAM (heparin-binding growth-associated molecule; pleiotrophin), which activates the cortactin-src kinase signaling pathway. This leads to rapid neurite extension in neuronal cells, which makes syndecan-3 as an interesting transmembrane receptor in neuronal development and regeneration. However, little is known about the signaling mechanism of syndecan-3. Here we have analyzed formation of ligand-N-syndecan signaling complexes at the cell surface using fluorescence resonance energy transfer (FRET) and bioluminescence resonance energy transfer (BRET). We show that ligand binding leads to dimerization of syndecan-3 at the cell surface. The dimerized syndecan-3 colocalizes with actin in the filopodia of cells. Several amino acid residues (K383, G392 and G396) in the transmembrane domain are shown to be important for the ligand-induced dimerization, whereas the cytosolic domain is not required for the dimerization.
Subject: 3112 Neurosciences
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