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Choi, S., Lee, E., Kwon, S., Park, H., Yi, J.Y., Kim, S., Han, I.O., Yun, Y. and Oh, E.S. (2005) Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4. The Journal of Cell Biology, 280, 42573-42579. doi:10.1074/jbc.M509238200

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• TITLE: Ligand-induced dimerization of syndecan-3 at the cell surface

  AUTHORS: Evgeny Kulesskiy, Sarka Tumova, Heikki Rauvala

  KEYWORDS: Syndecan-3; Dimerization; HB-GAM; Pleiotrophin; BRET; FRET

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.4 No.6A, June 20, 2013

  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.