Qs. Tian et al., FAS-ACTIVATED SERINE THREONINE KINASE (FAST) PHOSPHORYLATES TIA-1 DURING FAS-MEDIATED APOPTOSIS, The Journal of experimental medicine, 182(3), 1995, pp. 865-874
We have identified a serine/threonine kinase that is rapidly activated
during Fas-mediated apoptosis. Fas-activated serine/threonine kinase
(FAST) is phosphorylated on serine and threonine residues in Jurkat ce
lls. In response to Fas ligation, it is rapidly dephosphorylated and c
oncomitantly activated to phosphorylate TIA-1, a nuclear RNA-binding p
rotein that has been implicated as an effector of apoptosis. Phosphory
lation of TIA-1 precedes the onset of DNA fragmentation, suggesting a
role in signaling downstream events in the apoptotic program. Our resu
lts introduce FAST and TIA-1 as components of a molecular cascade invo
lved in signaling Fas-mediated apoptosis.