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Direct interaction of Frizzled‐1, ‐2, ‐4, and ‐7 with PDZ domains of PSD‐95
Author(s) -
Hering Heike,
Sheng Morgan
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02831-4
Subject(s) - frizzled , wnt signaling pathway , pdz domain , microbiology and biotechnology , biology , lrp6 , lrp5 , signal transduction , intracellular , receptor , genetics
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.