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Details on Person Like other classical cadherins, CDH11 associates with severa...
| Class:Id | Summation:9793108 |
|---|---|
| _displayName | Like other classical cadherins, CDH11 associates with severa... |
| _timestamp | 2022-06-09 20:25:25 |
| created | [InstanceEdit:9793109] Orlic-Milacic, Marija, 2022-06-02 |
| modified | [InstanceEdit:9793235] Orlic-Milacic, Marija, 2022-06-09 [InstanceEdit:9793236] Orlic-Milacic, Marija, 2022-06-09 |
| text | Like other classical cadherins, CDH11 associates with several catenin proteins through its intracellular domain, which is thought to play a role in the establishment and regulation of adherens junctions. These catenin proteins include CTNND1 (also known as p120 catenin or delta-catenin), CTNNB1 (beta-catenin), JUP (Junction Plakoglobin, also known as gamma-catenin), and CTNNA1 (alpha-catenin) (Straub et al. 2003; Kiener et al. 2006; Ortiz et al. 2015; Lee et al. 2018). CDH11, through its C terminus, also forms a complex with angiomotin (AMOT) isoform p80 (AMOT-2), which is implicated in CDH11-mediated cell migration and tumor cell invasiveness (Levchenko et al. 2004; Jiang et al. 2006; Yi et al. 2011; Ortiz et al. 2015; Lee et al. 2018). Through its extracellular region, CDH11 binds to the C terminal fragment of ANGPTL4 (Angiopoietin-like-4), commonly known as cANGPTL4, which is implicated in the regulation of wound healing. The variant isoform of CDH11 (CDH11v), an 85 kDa membrane-bound protein produced as a result of alternative splicing (Kawaguchi et al. 1999), can compete with the canonical CDH11 for cANGPTL4 binding (Teo et al. 2017). |
| (summation) | [Pathway:9762292] Regulation of CDH11 function [Homo sapiens] |
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