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The Small GTPase Ran pp 163–176Cite as

Ran Regulation by Ran GEF and Ran GAP

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Abstract

The Ras-related GTPase Ran was first isolated as a complex with the chromatin-associated protein RCC1 (Bischoff and Ponstingl, 1991a), which turned out to be its guanine nucleotide exchange factor (GEF; Bischoff and Ponstingl, 1991b). Ran was mainly found in the nucleus and hence was designated the Ras-related nuclear protein. Most other Ras-related GTPases are present in small total amounts per cell, but attain high local concentrations by attachment to cellular membranes at their sites of action. In contrast, Ran is readily soluble, free to move, and is one of the most abundant proteins in the nucleus. It forms and dissociates transport complexes, depending on the state of its bound nucleotide. Here, we focus on the regulators of this state.

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  1. Division for Molecular Biology of Mitosis, German Cancer Research Center, D-69120, Heidelberg, Germany

    F. Ralf Bischoff & Herwig Ponstingl

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  1. F. Ralf Bischoff
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  2. Herwig Ponstingl
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  1. New York University School of Medicine, New York, NY, USA

    Mark Rush  & Peter D’Eustachio  & 

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Bischoff, F.R., Ponstingl, H. (2001). Ran Regulation by Ran GEF and Ran GAP. In: Rush, M., D’Eustachio, P. (eds) The Small GTPase Ran. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1501-2_9

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  • DOI: https://doi.org/10.1007/978-1-4615-1501-2_9

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