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FAT1 cadherin is multiply phosphorylated on its ectodomain but phosphorylation is not catalysed by the four‐jointed homologue
Author(s) -
Sadeqzadeh Elham,
de Bock Charles E.,
O'Donnell Maureen R.,
Timofeeva Anna,
Burns Gordon F.,
Thorne Rick F.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.08.014
Subject(s) - ectodomain , phosphorylation , cadherin , phosphoserine , microbiology and biotechnology , biology , kinase , lotus japonicus , serine , biochemistry , gene , receptor , mutant , cell
The interaction between the Drosophila cadherins fat and dachsous is regulated by phosphorylation of their respective ectodomains, a process catalysed by the atypical kinase four‐jointed. Given that many signalling functions are conserved between Drosophila and vertebrate Fat cadherins, we sought to determine whether ectodomain phosphorylation is conserved in FAT1 cadherin, and also whether FJX1, the vertebrate orthologue of four‐jointed, was involved in such phosphorylation events. Potential Fj consensus phosphorylation motifs were identified in FAT1 and biochemical experiments revealed the presence of phosphoserine and phosphothreonine residues in its extracellular domain. However, silencing FJX1 did not influence the levels of FAT1 ectodomain phosphorylation, indicating that other mechanisms are likely responsible.