During processing in the endoplasmic reticulum (ER), the cyt...

created [InstanceEdit:9933679] Orlic-Milacic, Marija, 2025-01-02
dbId 9933680
displayName During processing in the endoplasmic reticulum (ER), the cyt...
literatureReference
modified [InstanceEdit:9936218] Orlic-Milacic, Marija, 2025-01-22
schemaClass Summation
text During processing in the endoplasmic reticulum (ER), the cytosolic tail of CDH1 (E-cadherin) undergoes phosphorylation on conserved serine residues (McEwen et al. 2014). The most likely kinase responsible for CDH1 cytoplasmic tail phosphorylation is Casein Kinase II (also known as CK2), as the cytosolic tail of CDH1 contains several evolutionarily conserved CK2 consensus target sites (S840, S853, and S855 in mouse, corresponding to S838, S851, and S853, respectively, in human CDH1), and as CK2 was shown to phosphorylate both mouse (Lickert et al. 2000) and human CDH1 (Serres et al. 2000; Catimel et al. 2006) in vitro as well as in vivo. Casein Kinase I (also known as CK1) was shown to phosphorylate CDH1 in vitro (Catimel et al. 2006). GSK3B (GSK3-beta) consensus target sites are also present in the cytosolic tail of CDH1 (Lickert et al. 2000; Huber and Weis 2001; McEwen et al. 2014) and were shown to undergo GSK3B-mediated phosphorylation, which is dependent on prior phosphorylation of CK2-target residues (Lickert et al. 2000). Phosphorylation of the cytosolic tail of CDH1 increases its affinity for CTNNB1 (Lickert et al. 2000; McEwen et al. 2014), promotes presentation of CDH1 on the plasma membrane (Serres et al. 2000; McEwen et al. 2014) and cell adhesion (Lickert et al. 2000; Serres et al. 2000); McEwen et al. 2014), and was also proposed to sequester CDH1 from the degradation machinery during its posttranslational processing (Huber and Weis 2001; McEwen et al. 2014). Phosphorylated serine residues in the cytosolic tail of CDH1 that are critical for CTNNB1 binding were reported to be S840, S846 and S847 in McEwen et al. 2014 (they correspond to S842, S848, and S848, respectively in mouse Cdh1), which differ from CK2 consensus sites. Further studies are needed to identify other kinases involved in phosphorylation of the CDH1 cytosolic tail.
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