ppDVL binds DAAM1

Stable Identifier
Reaction [binding]
Homo sapiens
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DAAM1 (Dishevelled-associated activator of morphogenesis) is a formin-homology protein that was identified in a yeast two-hybrid screen for interactors with the DVL PDZ domain (Habas et al, 2001). FH proteins play a well-characterized role in regulating cytoskeletal reorganization (reviewed in Aspenstrom, 2010). DAAM1 contains an N-terminal GTPase binding domain (GBD), two central proline-rich FH domains and a C-terminal diaphanous autoinhibitory domain (DAD). In the absence of a WNT signal, DAAM1 exists in an autoinhibited conformation mediated by an intramolecular interaction between the DBD and DAD regions (Habas et al, 2001; Liu et al, 2007). Upon WNT signaling, a direct interaction between the DAD of DAAM1 and the PDZ domain of DVL relieves the autoinhibition. In the activated conformation, DAAM1 may undergo FH-dependent oligomerization and had been shown to recruit RHOA in a GBD-dependent manner (Habas et al, 2001; Liu et al, 2007).
Literature References
PubMed ID Title Journal Year
11779461 Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1

Kato, Y, He, X, Habas, R

Cell 2001
19589360 Formin-binding proteins: modulators of formin-dependent actin polymerization

Aspenström, P

Biochim. Biophys. Acta 2010
18162551 Mechanism of activation of the Formin protein Daam1

Runnels, LW, Bharti, R, Khadka, D, Sato, A, Diaz, H, Habas, R, Liu, W

Proc Natl Acad Sci U S A 2008
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