Abstract

Protein limitation in vivo or amino acid deprivation of cells in culture causes a signal transduction cascade consisting of activation of the kinase GCN2 (general control nonderepressible 2), phosphorylation of eukaryotic initiation factor 2, and increased synthesis of activating transcription factor (ATF) 4 by a translational control mechanism. In a self-limiting transcriptional program, ATF4 transiently activates a wide range of downstream target genes involved in transport, cellular metabolism, and other cell functions. Simultaneous activation of other signal transduction pathways by amino acid deprivation led to the question of whether or not the increased abundance of ATF4 alone was sufficient to trigger the transcriptional control mechanisms. Using 293 cells that ectopically express ATF4 in a tetracycline-inducible manner showed that ATF4 target genes were activated in the absence of amino acid deprivation. Ectopic expression of ATF4 alone resulted in effective recruitment of the general transcription machinery, but some reduction in histone modification was observed. These data document that ATF4 alone is sufficient to trigger the amino acid-responsive transcriptional control program. However, the absolute amount of ectopic ATF4 required to achieve the same degree of transcriptional activation observed after amino acid limitation was greater, suggesting that other factors may serve to enhance ATF4 function.

Highlights

  • 3) Ectopically expressed activating transcription factor 4 (ATF4) causes the recruitment of the general transcription machinery in a manner indistinguishable from that triggered by the amino acid response (AAR). 4) To achieve the same level of transcription activity requires a significantly greater increase in ectopic ATF4 protein compared with that produced after AAR activation

  • The role of ATF4 as the primary activator is consistent with the high degree of conservation of the activating transcription factor (ATF) half-site (TGATG) within the C/EBP-ATF response element (CARE) composite sites that function as amino acid response elements [11]

  • It is possible that the binding of different basic region leucine zipper (bZIP) proteins at the disparate C/EBP half-site results in a gain of specificity for the general ATF4 activation signal

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Summary

Introduction

During the first stage, increased ATF4 synthesis leads to enhanced binding to the CARE composite sites This binding is associated with localized histone acetylation and subsequent recruitment of the general transcriptional machinery. During the second stage of the ATF4 response, increased expression of ATF3, C/EBP␤, and CHOP leads to their binding at the CARE site, which causes a subsequent suppression of transcription back toward the basal level. This self-limiting model for ATF4 action, originally reported for asparagine synthetase (ASNS), has been confirmed for several other CARE-containing genes [14, 18]

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