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Publication : Direct interaction of Frizzled-1, -2, -4, and -7 with PDZ domains of PSD-95.

First Author  Hering H Year  2002
Journal  FEBS Lett Volume  521
Issue  1-3 Pages  185-9
PubMed ID  12067714 Mgi Jnum  J:200324
Mgi Id  MGI:5508283 Doi  10.1016/s0014-5793(02)02831-4
Citation  Hering H, et al. (2002) Direct interaction of Frizzled-1, -2, -4, and -7 with PDZ domains of PSD-95. FEBS Lett 521(1-3):185-9
abstractText  In Drosophila, the frizzled gene plays a critical role in the establishment of tissue polarity, but the function of the Frizzled family of proteins in mammals is largely unknown. Recent evidence suggested that Frizzleds are receptors for the Wnt family of secreted glycoproteins which are involved in cell fate determination. However, it is unclear how Frizzled receptors transduce Wnt signals to intracellular signaling components. Here we show that the mouse Frizzled-1, -2, -4 and -7 can bind to proteins of the PSD-95 family, which are implicated in the assembly and localization of multiprotein signaling complexes in the brain. Moreover, PSD-95 can form a ternary complex with Frizzled-2 and the adenomatous polyposis coli protein, a negative regulator of Wnt signaling, suggesting that members of the PSD-95 family may serve to recruit intracellular signaling molecules of the Wnt/Frizzled pathway into the vicinity of the receptor.
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