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Characterization of HEK293T-SPINDOC KO vs WT by RNA-Seq profiling

ABSTRACT: Background: SPIN1 is a known histone code effector protein, which is composed of three Tudor domains. With its second Tudor domain, it reads the H3K4me3 mark, which is the canonical signal for transcriptional activation. It also has the ability to recognize combinatorial marks like H3R8me2a and H3K9me3 through its first Tudor domain, when they occur in the presence of K3K4me3. We identified SPINDOC as a stable component of the SPIN1 protein complex. SPINDOC referred to its ability to dock with SPIN1, which was previously called C11orf84 before it was functionally deorphanized. Objective: To investigate the biological function of SPINDOC, we generated SPINDOC KO by CRISPR technology in HEK293T cell lines and performed RNA sequencing. Conclusion:Our data represent the first detailed analysis of SPINDOC associated transcriptome, with biologic replicates, generated by RNA-seq technology. Comprehensive RNA-seq analysis demonstrated that 1005 genes were differentially regulated, including 459 up-regulated genes and 546 down-regulated genes.

ORGANISM(S): Homo sapiens

PROVIDER: GSE167306 | GEO | 2021/02/24

REPOSITORIES: GEO

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Evolving Spindlin1 Small Molecule Inhibitors Using Protein Microarrays

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A chemical probe for Tudor domain protein SPIN1 to investigate chromatin functions

Project description:A chemical probe for Tudor domain protein SPIN1 to investigate chromatin functions

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A chemical probe for Tudor domain protein SPIN1 to investigate chromatin functions

Project description:Lysine and arginine methylation are amongst the most frequent modifications on unstructured histone tails and in combination with other modifications provide the basis for a combinatorial 'chromatin or histone code'. Recognition of modified histone residues is accomplished in a specific manner by 'reader' domains that recognize chromatin modifications allowing to associate with specific effector complexes mediating chromatin functions. The methyl-lysine and methyl-arginine reader domain protein SPINDLIN1 (SPIN1) belongs to a family of 5 human genes, and has been identified as a putative oncogene and transcriptional co-activator containing three Tudor domains, able to mediate chromatin binding. Here we report on the discovery of the potent and selective bivalent Tudor domain inhibitor VinSPINIn, which simultaneously engages Tudor domains 1 and 2 and effectively competes with chromatin binding. Inhibitor, chemoproteomic and knockdown studies in squamous cell carcinoma suggest an un-anticipated complexity of SPIN isoform mediated interactions in regulating cellular phenotypes.

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