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ICLIP of GFP fusion proteins

ABSTRACT: iCLIP of GFP fusion proteins

PROVIDER: PRJEB12353 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	ERR1201430.fastq.gz	Fastqsanger.gz
	ERR1201440.fastq.gz	Fastqsanger.gz
	ERR1201431.fastq.gz	Fastqsanger.gz
	ERR1201441.fastq.gz	Fastqsanger.gz
	ERR1201432.fastq.gz	Fastqsanger.gz

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iCLIP of GFP fusion proteins

Project description:iCLIP of GFP fusion proteins

| PRJEB12353 | ENA

iCLIP of GFP fusion proteins

Project description:HeLa cells were cultured in DMEM, supplemented with 10% (v/v) FCS and penicillin/streptomycin under 5% CO2 at 37C. For iCLIP, HeLa cells expressing GFP fusion proteins were induced with doxycycline to adjust the level of recombinant protein to the level of the endogenous counterpart and irradiated with 150 mJ/cm2 UV light (254 nm). The iCLIP cDNA libraries were sequenced with 50 bp on an Illumina HiSeq 2000 instrument. RNASeq was performed as a control with 50 bp paired-end on an Illumina HiSeq 2000 instrument.

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Di- and trimeric biological switches made of nanobody-cytokine receptor fusion proteins simulate IL-23 signaling

Project description:Cytokine-induced signal transduction is executed by natural biological switches, which among many others control immune related processes. To construct a biological device, that simulates cytokine signaling, we utilized nanobodies to generate synthetic cytokine receptors (SyCyR). High affinity GFP- and mCherry-nanobodies were selected and extracellularly fused to trans-membrane and intracellular domains of IL-23 cytokine receptors. Soluble homo- and heterodimeric GFP:mCherry fusion proteins served as SyCyR ligands. Heterodimeric GFP-mCherry and homodimeric GFP fusion proteins efficiently phenocopied IL-23 signal transduction, respectively, as demonstrated by STAT3-, ERK- and Akt-activation, SOCS3 expression and transcriptome profiling. Interestingly, the homodimeric GFP fusion protein induced IL-23 receptor homo-dimerization and activation of IL-23-like signal transduction

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