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Abstract How paralogous proteins acquire distinct substrate specificities remains a central question in molecular evolution. We reveal an evolutionary switch in substrate targeting between LNX paralogs, E3 ubiquitin ligases that mediate proteasome-dependent degradation of the cell fate determinant NUMB. In teleost fish and amphibians, Numb degradation is primarily mediated by Lnx2, whereas Lnx1 exhibits minimal activity toward Numb.
Several different gene switches have been explored for their ability to precisely regulate transgene expression in cell culture and animal models, with varying degrees of success1,2,3.
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