High impact information on LOC396235

• Calcium-induced phosphorylation of ETS1 inhibits its specific DNA binding activity [1].
• Previous studies have shown that Ets1 becomes rapidly and transiently phosphorylated following antigen receptor (T cell (antigen) receptor (TCR) and membrane Ig) triggering a response which is absolutely dependent on ligand-induced calcium mobilization [1].
• This suggests that Ets1 contains one or more intrinsic transcription activation domain(s) [2].
• Ets1, the translation product of the c-ets1 proto-oncogene and the related Ets2 protein, act as sequence-specific transcriptional factors in transient transfection experiments in animal cells [2].
• In the present study, we show that during early organogenesis in the chick embryo, ETS1 mRNA expression was transiently induced in epithelial structures, during emigration of neural crest cells and dispersion of somites into the mesenchymal sclerotome [3].

Anatomical context of LOC396235

• Our data are consistent with a model in which the calcium-dependent phosphorylation of Ets1 represent the first step of a general clearance of Ets1 function during T and B cell activation [1].

Associations of LOC396235 with chemical compounds

• By a combination of two-dimensional tryptic phosphopeptide and mutational analyses, the target residues of these calcium-dependent phosphorylation events are identified as 4 serine residues clustered in a domain of Ets1 adjacent to its DNA binding domain (Ets domain) [1].

References