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Details on Person CBL-like E3 ubiquitin ligase Hakai (CBLL1) binds to SRC-phos...

Class:IdSummation:8876997
_displayNameCBL-like E3 ubiquitin ligase Hakai (CBLL1) binds to SRC-phos...
_timestamp2016-06-28 15:51:50
created[InstanceEdit:8876996] Orlic-Milacic, Marija, 2016-06-17
literatureReference[LiteratureReference:8876973] Successive post-translational modifications of E-cadherin are required for InlA-mediated internalization of Listeria monocytogenes
[LiteratureReference:8876930] Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex
[LiteratureReference:8876990] Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin
modified[InstanceEdit:8877122] Orlic-Milacic, Marija, 2016-06-20
[InstanceEdit:8877849] Orlic-Milacic, Marija, 2016-06-28
[InstanceEdit:8877852] Orlic-Milacic, Marija, 2016-06-28
textCBL-like E3 ubiquitin ligase Hakai (CBLL1) binds to SRC-phosphorylated E-cadherin (CDH1) complex bound to Listeria monocytogenes cell wall protein InlA (Bonazzi et al. 2008). SRC-mediated phosphorylation of CDH1 complex on tyrosine residues Y753 and Y754 of CDH1 and an unknown tyrosine of beta-catenin (CTNNB1) at cell-cell adhesion sites creates docking sites for CBLL1. CBLL1 functions as zinc (Zn2+) coordinated homodimer. While CBLL1 interacts simultaneously with CDH1 and CTNNB1, CTNND1 (p120 catenin) is displaced by CBLL1 binding (Fujita et al. 2002, Mukherjee et al. 2012).
(summation)[Reaction:8876993] CBLL1 binds SRC-phosphorylated CDH1 complex [Homo sapiens]
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