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First published online April 23, 2008
doi: 10.1242/10.1242/jcs.026401

Journal of Cell Science 121, 1349-1355 (2008)
Published by The Company of Biologists 2008
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The ins and outs of syntenin, a multifunctional intracellular adaptor protein

Jeffrey M. Beekman and Paul J. Coffer*

Departments of Immunology and Pediatric Immunology, Wilhelmina Children's Hospital, University Medical Center, Lundlaan 6, 3584 EA Utrecht, The Netherlands


Figure 1
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  		Fig. 1. The domain structure of syntenin and an overview of conserved N-terminal tyrosine residues. The N-terminal domain (NTD), the PDZ-domain tandem and the C-terminal domain of syntenin. Five tyrosine residues within the NTD (amino acids 1-66) are conserved, as indicated in the lower part of the figure. From these, Y4 and Y56 both consist of consensus ITIM motifs (both SxYxxL), whereas Y46 and Y56 resemble the ITAM motif (YxxLxxxxxxYxxL).

 

Figure 2
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  		Fig. 2. Syntenin-dependent subcellular trafficking of receptors and regulation by Rab- and Arf-family GTPases. Black arrows indicate syntenin-controlled trafficking of proTGF{alpha} in the secretory route, syndecans and CD63 in the endosomal compartment and tethering of Delta1 at the plasma membrane; grey arrows indicate syntenin-independent trafficking. Inhibitory activity of syntenin for trafficking through a particular route is also indicated. The regulators Rab5, Rab7, Rab11 and Arf6 (indicated in bold) have been reported to bind and/or colocalize with syntenin. The major composition of phosphoinositol lipids that are present in a particular organelle is indicated by the colour scheme in the key. The question mark indicates contradictory results. EE, early endosome; ER, endoplasmic reticulum; LE, late endosome; MVB, multivesicular body; RE, recycling endosome; TGN, trans-Golgi network.

 

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