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Ubiquitination of Rac1 by Inhibitors of Apoptosis (IAPs)

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Book cover Ras Signaling

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1120))

Abstract

Ubiquitination of proteins has emerged as a vital posttranslational modification at the crux of numerous signalling pathways, regulating them in various ways. Most members of the small GTPase family including Ras and Rho proteins are regulated by GEFs, GAPs, and RhoGDIs that modulate their cycling between the active and inactive states. Ubiquitination has added another layer to the regulation of small GTPases. Recently, we have uncovered that inhibitors of apoptosis (IAPs) function as direct E3 ubiquitin ligases for Rho GTPase Rac1 and target it for proteasomal degradation. Here, we describe in vitro and in vivo ubiquitination assays for detecting the conjugation of ubiquitin to Rac1 by XIAP and cIAP1.

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Acknowledgements

The work discussed here is supported through an ENP grant RA1739/1-1 to KR from the DFG. KR is a PLUS3 fellow of the Boehringer Ingelheim Foundation.

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Oberoi-Khanuja, T.K., Rajalingam, K. (2014). Ubiquitination of Rac1 by Inhibitors of Apoptosis (IAPs). In: Trabalzini, L., Retta, S. (eds) Ras Signaling. Methods in Molecular Biology, vol 1120. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-791-4_4

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  • DOI: https://doi.org/10.1007/978-1-62703-791-4_4

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-790-7

  • Online ISBN: 978-1-62703-791-4

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