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Baietti M.F.,Laboratory for Glycobiology and Developmental Genetics | Baietti M.F.,Laboratory for Signal Integration in Cell Fate Decision | Baietti M.F.,Center for the Biology of Disease | Zhang Z.,Laboratory for Glycobiology and Developmental Genetics | And 17 more authors.
Nature Cell Biology | Year: 2012

The biogenesis of exosomes, small secreted vesicles involved in signalling processes, remains incompletely understood. Here, we report evidence that the syndecan heparan sulphate proteoglycans and their cytoplasmic adaptor syntenin control the formation of exosomes. Syntenin interacts directly with ALIX through LYPX(n)L motifs, similarly to retroviral proteins, and supports the intraluminal budding of endosomal membranes. Syntenin exosomes depend on the availability of heparan sulphate, syndecans, ALIX and ESCRTs, and impact on the trafficking and confinement of FGF signals. This study identifies a key role for syndecan-syntenin-ALIX in membrane transport and signalling processes. © 2012 Macmillan Publishers Limited. All rights reserved.

Wawrzyniak A.M.,Laboratory for Signal Integration in Cell Fate Decision | Vermeiren E.,Laboratory for Signal Integration in Cell Fate Decision | Zimmermann P.,Laboratory for Signal Integration in Cell Fate Decision | Ivarsson Y.,Laboratory for Signal Integration in Cell Fate Decision
FEBS Letters | Year: 2012

Syntenin-1 is a PDZ protein involved in receptor recycling and clustering. Its two PDZ domains interact with various receptors and phosphoinositides, and are flanked by N- and C-terminal regions. Here, we report the identification of an autoinhibitory peptide stretch in the N-terminus that might be regulated by phosphorylation. We further establish that basic residues in the C-terminal region mediate electrostatic interactions with reconstituted liposomes and contribute to the plasma membrane targeting. Our study adds new components to the multi-dentate membrane targeting mechanism and highlights the role of N- and C-terminal PDZ extensions in the regulation of syntenin-1 plasma membrane localization. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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