PDZ Tandem of Human Syntenin
2003; Elsevier BV; Volume: 11; Issue: 4 Linguagem: Inglês
10.1016/s0969-2126(03)00052-2
ISSN1878-4186
AutoresBeom Sik Kang, David R. Cooper, Filip Jeleń, Y. Devedjiev, Urszula Derewenda, Zbigniew Dauter, Jacek Otlewski, Zygmunt S. Derewenda,
Tópico(s)Wnt/β-catenin signaling in development and cancer
ResumoSyntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin.
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