Pertussis toxin. Entry into cells and enzymatic activity

In this study we present data supporting the concept of a retrograde transport mechanism for pertussis toxin to the Golgi complex. We also describe a novel GTP-binding 32 kDa cellular target protein, which is ADP-ribosylated upon exposure to PT and different from the classical PT substrate, the alph...

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Bibliographic Details
Published in:	Advances in experimental medicine and biology Vol. 419; p. 83
Main Authors:	el Bayâ, A, Linnermann, R, von Olleschik-Elbheim, L, Schmidt, M A
Format:	Journal Article
Language:	English
Published:	United States 1997
Subjects:	Adenosine Diphosphate Ribose - metabolism Animals Biological Transport Cell Line CHO Cells Cricetinae Dogs GTP-Binding Protein alpha Subunits, Gi-Go - metabolism Pertussis Toxin Virulence Factors, Bordetella - metabolism
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Summary:	In this study we present data supporting the concept of a retrograde transport mechanism for pertussis toxin to the Golgi complex. We also describe a novel GTP-binding 32 kDa cellular target protein, which is ADP-ribosylated upon exposure to PT and different from the classical PT substrate, the alpha-subunit of Gi proteins.
ISSN:	0065-2598
DOI:	10.1007/978-1-4419-8632-0_9