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The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway

ABSTRACT: The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway

PROVIDER: PRJNA246553 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR1282280_1.fastq.gz	Fastqsanger.gz
	SRR1282280_2.fastq.gz	Fastqsanger.gz
	SRR1282281_1.fastq.gz	Fastqsanger.gz
	SRR1282281_2.fastq.gz	Fastqsanger.gz
	SRR1282273.fastq.gz	Fastqsanger.gz

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The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway [RNA-Seq]

Project description:The aim of this study is to identify the SPIN1 target genes in liposarcoma cells

2017-02-09 | GSE57501 | GEO

The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway [ChIP-Seq]

Project description:The aim of this study is to identify the SPIN1 target genes in liposarcoma cells

2017-02-09 | GSE57499 | GEO

The histone code reader SPIN1 controls RET signaling in liposarcoma.

Project description:The histone code reader Spindlin1 (SPIN1) has been implicated in tumorigenesis and tumor growth, but the underlying molecular mechanisms remain poorly understood. Here, we show that reducing SPIN1 levels strongly impairs proliferation and increases apoptosis of liposarcoma cells in vitro and in xenograft mouse models. Combining signaling pathway, genome-wide chromatin binding, and transcriptome analyses, we found that SPIN1 directly enhances expression of GDNF, an activator of the RET signaling pathway, in cooperation with the transcription factor MAZ. Accordingly, knockdown of SPIN1 or MAZ results in reduced levels of GDNF and activated RET explaining diminished liposarcoma cell proliferation and survival. In line with these observations, levels of SPIN1, GDNF, activated RET, and MAZ are increased in human liposarcoma compared to normal adipose tissue or lipoma. Importantly, a mutation of SPIN1 within the reader domain interfering with chromatin binding reduces liposarcoma cell proliferation and survival. Together, our data describe a molecular mechanism for SPIN1 function in liposarcoma and suggest that targeting SPIN1 chromatin association with small molecule inhibitors may represent a novel therapeutic strategy.

| S-EPMC4467114 | biostudies-literature

The histone code reader Spin1 controls skeletal muscle development

Project description:We report developmental defects in Spin1(Myf5-Cre) mice, in which Spin1 is ablated in skeletal muscle.

2017-12-08 | GSE92539 | GEO

The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway

Project description:This SuperSeries is composed of the SubSeries listed below.

2017-02-09 | GSE57502 | GEO

Homo sapiens

Project description:The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway [ChIP-Seq]

| PRJNA246554 | ENA

Homo sapiens

Project description:The epigenetic reader protein SPIN1 controls proliferation and survival of liposarcoma by modulating the RET signaling pathway [RNA-Seq]

| PRJNA246555 | ENA

The intrinsically disordered region of SPIN1 regulates its function by phase separation [ChIP-seq]

Project description:As a transcriptional coactivator, SPIN1 has been reported to bind to chromatin.To assess the effect of IDR on chromatin binding, we investigated genome-wide chromatin association of SPIN1-WT or SPIN1-△IDR stably overexpressed cell lines by chromatin immunoprecipitation followed by high-throughput sequencing.

2024-12-19 | GSE215398 | GEO

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* (see Footnote), 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.

2022-02-23 | PXD011703 | Pride

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.

2018-11-29 | GSE123084 | GEO

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