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Biology subjects

Genisson, Y.

Publications and source records attributed to Genisson, Y..

2 recordsLinked to original sources

Exploiting HSD17B11-dependent dialkynylcarbinols cytotoxicity for facile CRISPR/Cas9-based gene inactivation

Several approaches have been developed to improve the efficiency of CRISPR/Cas9-based genome editing, including the co-inactivation of a gene whose loss confers resistance to a cytotoxic compound, thereby enabling enrichment of successfully edited cells. Here, we show across multiple cell lines that inactivation of HSD17B11, a non-essential member of the Short-chain Dehydrogenase/Reductase (SDR) superfamily, confers strong resistance (29- to 131-fold) to a Phenyl diAlkynylCarbinol compound (PAC) in both human and mouse cells, without affecting cell viability or proliferation. We demonstrate that co-inactivation of HSD17B11 followed by PAC selection can be used to rapidly identify efficient guide RNAs targeting a gene of interest and to readily isolate clones inactivated for one or multiple genes. Altogether, these results establish a simple and efficient experimental strategy for generating knockout cells by using PAC selection to enrich for successfully edited cells.

molecular biology↗

SDR enzymes oxidize specific lipidic alkynylcarbinols into cytotoxic protein-reactive species

Hundreds of cytotoxic natural or synthetic lipidic compounds contain chiral alkynylcarbinol motifs, but the mechanism of action of those potential therapeutic agents remains unknown. Using a genetic screen in haploid human cells, we discovered that the enantiospecific cytotoxicity of numerous terminal alkynylcarbinols, including the highly cytotoxic dialkynylcarbinols, involves a bioactivation by HSD17B11, a short-chain dehydrogenase/reductase (SDR) known to oxidize the C-17 carbinol center of androstan-3-alpha,17-beta-diol to the corresponding ketone. A similar oxidation of dialkynylcarbinols generates dialkynylketones, that we characterize as highly protein-reactive electrophiles. We established that, once bioactivated in cells, the dialkynylcarbinols covalently modify several proteins involved in protein-quality control mechanisms, resulting in their lipoxidation on cysteines and lysines through Michael addition. For some proteins, this triggers their association to cellular membranes and results in endoplasmic reticulum stress, unfolded protein response activation, ubiquitin-proteasome system inhibition and cell death by apoptosis. Finally, as a proof-of-concept, we show that generic lipidic alkynylcarbinols can be devised to be bioactivated by other SDRs, including human RDH11 and HPGD/15-PGDH. Given that the SDR superfamily is one of the largest and most ubiquitous, this unique cytotoxic mechanism-of-action could be widely exploited to treat diseases, in particular cancer, through the design of tailored prodrugs. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=108 SRC="FIGDIR/small/460423v1_ufig1.gif" ALT="Figure 1"> View larger version (47K): org.highwire.dtl.DTLVardef@12daae1org.highwire.dtl.DTLVardef@12db406org.highwire.dtl.DTLVardef@1863517org.highwire.dtl.DTLVardef@7b548_HPS_FORMAT_FIGEXP M_FIG Graphical abstract C_FIG

biochemistry↗