CTNNB1 dissociates from CDH11 upon ANGPTL4 binding

Stable Identifier
R-HSA-9762282
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Binding of the C-terminal fragment of angiopoietin-like 4, commonly known as cANGPTL4 and in this diagram labeled as ANGPTL4(164-406), to the extracellular region of CDH11 leads to release of CDH11-bound CTNNB1 (beta-catenin) to the cytosol. This CTNNB1 release is independent of activation of WNT receptors. cANGPTL4 upregulates transcription of ID3 (Inhibitor of DNA-binding/differentiation protein 3) in a CDH11- and CTNBB1-dependent manner. ID3 forms a complex with a basic helix-loop-helix (bHLH) transcription factor scleraxis (SCX), and this complex inhibits scar-associated production of collagens COL1A2 and COL3A1 by fibroblasts (Teo et al. 2017). The variant isoform of CDH11 (CDH11v), which does not possess the cytoplasmic domain and does not bind CTNNB1, can compete with the canonical CDH11 for cANGPTL4 binding, leading to diminished CTNNB1 release (Teo et al. 2017).
Literature References
PubMed ID Title Journal Year
28740178 Angiopoietin-like 4 induces a β-catenin-mediated upregulation of ID3 in fibroblasts to reduce scar collagen expression

Teo, DJR, Sng, MK, Teo, Z, Zhu, P, Chong, HC, Tan, NS, Chan, JSK, Wong, MTC, Phua, GZM, Choo, CC, Choong, C

Sci Rep 2017
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