MassIVE MSV000091134

Partial Public

Simultaneous substrate and ubiquitin modification recognition by bispecific antibodies allows detection of ubiquitinated RIP1 and RIP2

Description

Ubiquitination is crucial for the dynamic regulation of diverse signaling pathways. To enhance understanding of ubiquitination mediated signaling, we generated a new class of bispecific antibodies which combine recognition of ubiquitination substrates and specific polyubiquitin linkages. RIP1-K63 or RIP1-linear (Lin) linkage polyubiquitin bispecific antibodies can detect linkage-specific RIP1 ubiquitination in cells and in tissues, and also reveal RIP1 ubiquitination by immunofluorescence. In a similar fashion, RIP2 ubiquitination with K63 or linear linkages can be specifically detected with RIP2-K63 and RIP2-Lin bispecific antibodies. Furthermore, using RIP2-K63 and RIP2- Lin bispecific antibodies we examined IBD patient samples and found prominent K63- linked and linear RIP2 ubiquitination in ulcerative colitis and Crohn's disease patient samples. We also developed a bispecific antibody (K63-Lin) that can simultaneously recognize K63-linked and linear ubiquitination in a variety of signaling pathways. Collectively, these bispecific antibodies provide a novel conceptual paradigm for potential future development of inflammatory markers. [doi:10.25345/C5SB3X800] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: ubiquitination

Contact

Principal Investigators:
(in alphabetical order)
Domagoj Vucic, Genentech, United States
Submitting User: coreyeb
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