Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis

Qingsheng Tian, Jean Luc Taupin, Stephen Elledge, Michael Robertson, Paul Anderson

Research output: Contribution to journalArticle

145 Citations (Scopus)

Abstract

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 cells. In response to Fas ligation, it is rapidly dephosphorylated and concomitantly activated to phosphorylate TIA-1, a nuclear RNA-binding protein that has been implicated as an effector of apoptosis. Phosphorylation of TIA-1 precedes the onset of DNA fragmentation, suggesting a role in signaling downstream events in the apoptotic program. Our results introduce FAST and TIA-1 as components of a molecular cascade involved in signaling Fas-mediated apoptosis.

Original languageEnglish (US)
Pages (from-to)865-874
Number of pages10
JournalJournal of Experimental Medicine
Volume182
Issue number3
DOIs
StatePublished - Sep 1 1995
Externally publishedYes

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Protein-Serine-Threonine Kinases
Apoptosis
Nuclear RNA
Jurkat Cells
RNA-Binding Proteins
DNA Fragmentation
Threonine
Nuclear Proteins
Serine
Ligation
Phosphorylation

ASJC Scopus subject areas

  • Immunology

Cite this

Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis. / Tian, Qingsheng; Taupin, Jean Luc; Elledge, Stephen; Robertson, Michael; Anderson, Paul.

In: Journal of Experimental Medicine, Vol. 182, No. 3, 01.09.1995, p. 865-874.

Research output: Contribution to journalArticle

Tian, Qingsheng ; Taupin, Jean Luc ; Elledge, Stephen ; Robertson, Michael ; Anderson, Paul. / Fas-activated serine/threonine kinase (FAST) phosphorylates TIA-1 during Fas-mediated apoptosis. In: Journal of Experimental Medicine. 1995 ; Vol. 182, No. 3. pp. 865-874.
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