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Regulation of the Activity of Eukaryotic Initiation Factors in Stressed Cells

  • Chapter
Signaling Pathways for Translation

Part of the book series: Progress in Molecular and Subcellular Biology ((PMSB,volume 27))

Abstract

Exposure of cells to elevated temperatures, also known as heat shock, or exposure to other kinds of environmental stress, gives rise to a general inhibition of protein synthesis, on the one hand, and to the increased synthesis of a group of chaperone proteins, on the other hand (Rhoads and Lamphear 1995; Duncan 1996). These chaperone proteins or heat shock proteins (HSPs) function mainly in folding and refolding of denatured or newly synthesized proteins and therefore counteract the toxic effects of denatured proteins on the cell (Wu 1995). The inhibition of protein synthesis is achieved by a reduced initiation of translation through the inactivation of various eukaryotic initiation factors (eIFs; Duncan 1996). Most studies have implicated the inactivation of eIF2, which is involved in the delivery of the initiator methionyl tRNA to the small ribosomal subunit, and the inactivation of eIF4E, a key component in the binding of several initiation factors to the mRNA, as the main causes of the reduced levels of initiation (e.g., Duncan and Hershey 1989; Duncan et al. 1995; Feigenblum and Schneider 1996; Scheper et al. 1997; Wang et al. 1998)

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  1. Gert C. Scheper

    Present address: Department of Anatomy and Physiology, University of Dundee, Dundee, DD1 5EH, Scotland

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  1. Department of Molecular Cell Biology, Utrecht University, Utrecht, The Netherlands

    Gert C. Scheper, Roel Van Wijk & Adri A. M. Thomas

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  1. Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA, 71130, USA

    Robert E. Rhoads

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Scheper, G.C., Van Wijk, R., Thomas, A.A.M. (2001). Regulation of the Activity of Eukaryotic Initiation Factors in Stressed Cells. In: Rhoads, R.E. (eds) Signaling Pathways for Translation. Progress in Molecular and Subcellular Biology, vol 27. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-09889-9_2

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