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Exogenous SLFN12 reduces in vivo TNBC proliferation and invasion, increases luminal markers and a gene signature that reducts better breast cancer survival in cohort database analysis

ABSTRACT: Exogenous SLFN12 reduces in vivo TNBC proliferation and invasion, increases luminal markers and a gene signature that reducts better breast cancer survival in cohort database analysis

PROVIDER: PRJNA890280 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21896021_1.fastq.gz	Fastqsanger.gz
	SRR21896021_2.fastq.gz	Fastqsanger.gz
	SRR21896022_1.fastq.gz	Fastqsanger.gz
	SRR21896022_2.fastq.gz	Fastqsanger.gz
	SRR21896023_1.fastq.gz	Fastqsanger.gz

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Exogenous SLFN12 reduces in vivo TNBC proliferation and invasion, increases luminal markers and a gene signature that reducts better breast cancer survival in cohort database analysis

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Project description:Garvie CW, Wu X, Papanastasiou M, Lee S, Fuller J, Schnitzler GR, Horner SW, Baker A, Zhang T, Mullahoo JP, Westlake L, Hoyt SH, Toetzl M, Ranaghan M, de Waal L, McGaunn J, Kaplan B, Piccioni F, Yang X, Lange M, Tersteegen A, Raymond D, Lewis TA, Carr SA, Cherniack AD, Lemke C, Meyerson M, Greulich H. 2021. DNMDP and related compounds, or "velcrins", induce complex formation between the phosphodiesterase PDE3A and the SLFN12 protein, leading to a cytotoxic response in cancer cells that express elevated levels of both proteins. The mechanisms by which velcrins induce complex formation, and how the PDE3A-SLFN12 complex causes cancer cell death, are not fully understood. Here, we show that PDE3A and SLFN12 form a heterotetramer stabilized by binding of DNMDP. Interactions between the C-terminal alpha helix of SLFN12 and residues near the active site of PDE3A are required for complex formation, and are further stabilized by interactions between SLFN12 and DNMDP. Moreover, we demonstrate that SLFN12 is an RNase, that PDE3A binding increases SLFN12 RNase activity, and that SLFN12 RNase activity is required for DNMDP response. This new mechanistic understanding will facilitate development of velcrin compounds into new cancer therapies.

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