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Bacterial Protein Toxins Acting on Small GTPases

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Ras Superfamily Small G Proteins: Biology and Mechanisms 1

Abstract

Numerous bacterial protein toxins and effectors target eukaryotic cells by covalent modification of low molecular mass GTP-binding proteins to manipulate their switch functions. Frequent targets are Rho, Ras, and Rab proteins which are modified by ADP-ribosylation, adenylylation, mono-O-glycosylation, deamidation, transglutamination, phosphocholination, and proteolytic cleavage. Thereby, the GTPases are activated or inactivated. Other bacterial effectors manipulate the cellular functions of small GTPases by mimicking endogenous regulators of the switch proteins. They act as guanine nucleotide exchange factors (GEFs) or GTPase-activating proteins (GAPs). The chapter describes the bacterial toxins and effectors and discusses the functional consequences of their actions.

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Notes

  1. 1.

    Here, toxins are designated as bacterial factors which are released from bacteria into the environment and then enter target cells independently of the pathogen. In contrast, bacterial effectors are introduced into host cells by an injection machinery of the bacteria as a result of direct contact of the pathogen with host cells.

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Acknowledgments

Authors’ studies reported were financially supported by the Deutsche Forschungsgemeinschaft.

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    Klaus Aktories & Gudula Schmidt

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    Alfred Wittinghofer

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Aktories, K., Schmidt, G. (2014). Bacterial Protein Toxins Acting on Small GTPases. In: Wittinghofer, A. (eds) Ras Superfamily Small G Proteins: Biology and Mechanisms 1. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1806-1_4

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