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Published 31 March 2003. doi:10.1083/jcb.200303032
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© The Rockefeller University Press, 0021-9525/2003/3/991 $5.00
The Journal of Cell Biology, Volume 160, Number 7, 991-992

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To be helped or not helped, that is the question



Emmanuel Lemichez and Patrice Boquet

INSERM U452, Faculty of Medicine, 28 avenue de Valombrose, 06107 Nice Cedex 2, France

Address correspondence to Patrice Boquet, INSERM U452, Faculty of Medicine, 28 avenue de Valombrose, 06107 Nice Cedex 2, France. Tel.: 33-4-93-37-77-09. Fax: 33-4-93-53-35-09. E-mail: boquet{at}unice.fr

Diphtheria toxin (DT)* is the paradigm of the powerful A-B toxins. These bacterial poisons bind to cells, are endocytosed, and inject their catalytic domain into the cytosol causing the irreversible modification of a key component of the the host cellular machinery. The mechanism by which the hydrophilic enzymatic fragment of DT crosses the endosomal membrane and is released into the cytosol remains controversial. In this issue, Ratts et al. (2003) demonstrate that delivery of the DT catalytic domain from the lumen of purified early endosomes to the external medium requires the addition of a cytosolic translocation factor complex composed in part of Hsp90 and thioredoxin reductase.

* Abbreviations used in this paper: DT, diphtheria toxin; DT-C, DT catalytic fragment; DT-T, DT transmembrane; EF-2, elongation factor 2.


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