The neuronal proteins CIPP, Cypin and IRSp53 form a tripartite complex mediated by PDZ and SH3 domains
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Manuela Barilari
Abstract
Here we report the dissection of a tripartite complex formed by CIPP (channel-interacting PDZ protein), IRSp53 (insulin receptor tyrosine kinase substrate protein) and Cypin (cytosolic PSD-95 interactor) in cultured cells. The three proteins are expressed in similar neuronal districts, where CIPP binds to different membrane channels and receptors, IRSp53 regulates the morphogenesis of actin-rich dendritic spines, and Cypin promotes dendrite branching and patterning by binding to tubulin heterodimers. We observed that the interaction among the three proteins is mediated by small binding domains: CIPP works as a bridge, linking the carboxy-termini of IRSp53 and Cypin with its PDZ domains; IRSp53 connects Cypin, through an unusual SH3-mediated association, which can be impaired by substituting two crucial positively charged residues of Cypin. The observation that the three engineered proteins co-localize in the cytoplasm, and at the tip of induced neurites in neuronal cells, raises the interesting possibility that they work together in the formation of neuronal protrusions.
©2010 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Guest Editorial
- Highlight: The Biology of Aging: Mechanisms and Intervention
- Highlight: 61th Mosbach Colloquium of the GBM ‘The Biology of Aging: Mechanisms and Intervention’
- Multiplex analysis of mitochondrial DNA pathogenic and polymorphic sequence variants
- The hypoxia-inducible factor HIF-1 functions as both a positive and negative modulator of aging
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- Glucose homeostasis and insulin sensitivity in growth hormone-transgenic mice: a cross-sectional analysis
- PROTEIN STRUCTURE AND FUNCTION
- New structural aspects of FKBP38 activation
- The neuronal proteins CIPP, Cypin and IRSp53 form a tripartite complex mediated by PDZ and SH3 domains
- CELL BIOLOGY AND SIGNALING
- Inhibition of interferon-α-induced signaling by hyperosmolarity and hydrophobic bile acids
- Role of the second disulfide bridge (Cys18-Cys274) in stabilizing the inactive AT1 receptor
- Demonstration of protein absorption in the intestinal epithelium of fish and mice by laser scanning confocal microscopy
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