- Title
- FAT1 cadherin is multiply phosphorylated on its ectodomain but phosphorylation is not catalysed by the four-jointed homologue
- Creator
- Sadeqzadeh, Elham; de Bock, Charles E.; O'Donnell, Maureen R.; Timofeeva, Anna; Burns, Gordon F.; Thorne, Rick F.
- Relation
- FEBS Letters Vol. 588, Issue 18, p. 3511-3517
- Publisher Link
- http://dx.doi.org/10.1016/j.febslet.2014.08.014
- Publisher
- Elsevier BV
- Resource Type
- journal article
- Date
- 2014
- Description
- 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.
- Subject
- ectodomain phosphorylation; fat cadherin; FAT1; FJX1; four-jointed; four-jointed box protein 1
- Identifier
- http://hdl.handle.net/1959.13/1296840
- Identifier
- uon:19310
- Identifier
- ISSN:0014-5793
- Language
- eng
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