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Human hnRNP H1 knockdown proteomics

ABSTRACT: HNRNP1 was characterized in a multi-dimensional study involving RNAi knockdown of the protein in HeLa cells. Label-free proteomics was used to characterize protein expression changes.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Cervix Carcinoma

SUBMITTER: Christine Vogel

LAB HEAD: Christine Vogel

PROVIDER: PXD000895 | Pride | 2016-01-25

REPOSITORIES: Pride

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			Action	DRS
	120120_C1_CYT.raw	Raw
	120120_C1_NF.raw	Raw
	120120_C2_CYT.raw	Raw
	120120_C2_NF.raw	Raw
	120120_HNRNPH2_CYT.raw	Raw

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Publications

High-throughput analyses of hnRNP H1 dissects its multi-functional aspect.

Uren Philip J PJ Bahrami-Samani Emad E de Araujo Patricia Rosa PR Vogel Christine C Qiao Mei M Burns Suzanne C SC Smith Andrew D AD Penalva Luiz O F LO

RNA biology 20160113 4

hnRNPs are polyvalent RNA binding proteins that have been implicated in a range of regulatory roles including splicing, mRNA decay, translation, and miRNA metabolism. A variety of genome wide studies have taken advantage of methods like CLIP and RIP to identify the targets and binding sites of RNA binding proteins. However, due to the complex nature of RNA-binding proteins, these studies are incomplete without assays that characterize the impact of RBP binding on mRNA target expression. Here we ...[more]

PMID: 26760575

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QUANTITATIVE SUBCELLULAR PROTEOMICS OF THE ORBITOFRONTAL CORTEX OF SCHIZOPHRENIA PATIENTS

Project description:We analyzed orbitofrontal cortex post-mortem brain tissue from patients. We generated an organellar proteome map from different subcellular fractions such as mitochondria (MIT), crude nuclear fraction (NUC) and cytoplasm (CYT) with the aim to monitor the subproteome changes using iTRAQ labelling for relative quantification and Selected Reaction Monitoring (SRM) for targeted quantification.

2019-10-10 | PXD014284 | Pride

QUANTITATIVE SUBCELLULAR PROTEOMICS OF THE ORBITOFRONTAL CORTEX OF SCHIZOPHRENIA PATIENTS

Project description:We analyzed OFC post-mortem brain tissue from patients classified as residual schizophrenia according to the DMS-IV manual. In this classification, the patients do not manifest prominent positive psychotic symptoms but prevail characteristic disturbance of negative symptoms. Through the comparison of patient´s samples against a pool of control subjects without any history of psychiatric illness we generated an organellar proteome map from different subcellular fractions such as mitochondria (MIT), crude nuclear fraction (NUC) and cytoplasm (CYT) with the aim to monitor the subproteome changes using iTRAQ labelling for relative quantification and Selected Reaction Monitoring (SRM) for targeted quantification.

2019-10-07 | PXD014350 | Pride

Transcriptome-wide mapping of hnRNP C and U2AF65 using iCLIP

Project description:iCLIP experiment to assess the binding of the highly abundant nuclear RNA-binding protein hnRNP C and core splicing factor U2AF65 on a genomic scale. To investigate how both proteins compete for binding at a subset of sites, U2AF65 iCLIP experiments were performed from both HNRNPC knockdown and control HeLa cells.

2013-01-31 | E-MTAB-1371 | biostudies-arrayexpress

Expression signatures of human HeLa cells with RNAi targetting A1 hnRNP, FUS, H hnRNP and p68-DDX5

Project description:Transcription profiling of human HeLa cells (cervical cancer cell line) transfected with a plasmid expressing shRNAs cloned into the pSuper expression vector compared to emprty vector negative controls for transfection. Four different RNA interference treatments targetted: A1 hnRNP (HNRNPA1, Heterogeneous nuclear ribonucleoprotein A1); FUS (fusion gene, involved in t(12;16) in malignant liposarcoma); H hnRNP (HNRNPH1); and p68 helicase (DDX5, DEAD (Asp-Glu-Ala-Asp) box polypeptide 5). Keywords: genetic modification Five-condition experiment, where HNRNPA1, FUS, HNRNPH1 and DDX5 gene product levels were inhibited by siRNA transfection and compared to transfection with the negative control (scrambled siRNA). Biological replicates: 2 of each of the first three treatments and 3 of the treatment against DDX5, all independently grown and harvested. No technical replicates were performed.

2008-08-20 | E-GEOD-12058 | biostudies-arrayexpress

High-throughput analyses of hnRNP H1 dissects its multi-functional aspect.

Project description:hnRNPs are polyvalent RNA binding proteins that have been implicated in a range of regulatory roles including splicing, mRNA decay, translation, and miRNA metabolism. A variety of genome wide studies have taken advantage of methods like CLIP and RIP to identify the targets and binding sites of RNA binding proteins. However, due to the complex nature of RNA-binding proteins, these studies are incomplete without assays that characterize the impact of RBP binding on mRNA target expression. Here we used a suite of high-throughput approaches (RIP-Seq, iCLIP, RNA-Seq and shotgun proteomics) to provide a comprehensive view of hnRNP H1s ensemble of targets and its role in splicing, mRNA decay, and translation. The combination of RIP-Seq and iCLIP allowed us to identify a set of 1,086 high confidence target transcripts. Binding site motif analysis of these targets suggests the TGGG tetramer as a prevalent component of hnRNP H1 binding motif, with particular enrichment around intronic hnRNP H1 sites. Our analysis of the target transcripts and binding sites indicates that hnRNP H1s involvement in splicing is 2-fold: it directly affects a substantial number of splicing events, but also regulates the expression of major components of the splicing machinery and other RBPs with known roles in splicing regulation. The identified mRNA targets displayed function enrichment in MAPK signaling and ubiquitin mediated proteolysis, which might be main routes by which hnRNP H1 promotes tumorigenesis.

| S-EPMC4841607 | biostudies-literature

Cohesin and Polycomb proteins functionally interact to control transcription at silenced, restrained, and active genes [expression array data]

Project description:Cohesin is crucial for proper chromosome segregation, but also regulates gene transcription and organism development by poorly understood mechanisms. We find that in Drosophila, cohesin functionally interacts with Polycomb group (PcG) silencing proteins at both silenced and active genes. Cohesin unexpectedly facilitates binding of Polycomb Repressive Complex 1 (PRC1) to many active genes. In contrast, cohesin and PRC1 binding are mutually antagonistic at silenced genes. PRC1 depletion decreases phosphorylated RNA polymerase and mRNA at many active genes, but increases them at silenced genes. Cohesin also facilitates long-range interactions between Polycomb Response Elements in the invected-engrailed gene complex where it represses transcription. These multiple distinct cohesin-PcG interactions reveal a previously unrecognized role for PRC1 in facilitating productive gene transcription, and provide new insights into how cohesin and PRC1 control development. We extracted RNA from control and Ph RNAi-treated BG3 cells and measured changes in gene expression following Ph dose depletion by hybridization to Affymetrix arrays. We also extracted RNA from wild-type wing imaginal disc and measured control wing disc expression levels by hybridization to Affymetrix arrays.

2013-04-25 | E-GEOD-42105 | biostudies-arrayexpress

hnRNP A1 iCLIP

Project description:This experiment identifies hnRNP A1 binding sites transcriptome-wide in Hela cells. HeLa cells with inducible expression of T7-tagged hnRNP A1 were grown to approximately 90% confluence and then subject to iCLIP analysis (following the protocol from Huppertz et al. 2014 (iCLIP: protein-RNA interactions at nucleotide resolution)). The iCLIP library was sequenced using Illumina's HighSeq 1500

2016-06-23 | E-MTAB-3612 | biostudies-arrayexpress

Autoregulatory circuit of human rpL3 expression requires hnRNP H1, NPM and KHSRP.

Project description:Alternative pre-mRNA splicing (AS) is a major mechanism that allows proteomic variability in eukaryotic cells. However, many AS events result in mRNAs containing a premature termination codon, which are degraded by nonsense-mediated mRNA decay (NMD) pathway. We have previously demonstrated that human rpL3 autoregulates its expression through the association of AS with NMD. In fact, overexpression of rpL3 promotes downregulation of canonical splicing and upregulation of alternative splicing that produces an NMD-targeted mRNA isoform. The result of these events is a decreased production of rpL3. We have also identified heterogeneous nuclear ribonucleoprotein (hnRNP) H1 as a splicing factor involved in the regulation of rpL3 alternative splicing and identified its regulatory cis-elements within intron 3 transcript. Here, we report that NPM and KHSRP are two newly identified proteins involved in the regulation of rpL3 gene expression via AS-NMD. We demonstrate that hnRNP H1, KHSRP and NPM can be found associated, and present also in ribonucleoproteins (RNPs) including rpL3 and intron 3 RNA in vivo, and describe protein-protein and RNA-protein interactions. Moreover, our data provide an insight on the crucial role of hnRNP H1 in the regulation of the alternative splicing of the rpL3 gene.

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SRSF3 and hnRNP H1 regulate a splicing hotspot of HER2 in breast cancer cells.

Project description:Overexpression of the oncogene HER2 occurs in 20-30% of invasive breast cancer and is associated with poor prognosis. A number of different splice variants of HER2 have been identified which produce functionally different proteins. Previously these splice variants have been investigated separately, but in the present study we collectively look at the expression and regulation of a group of HER2 splice variants produced by a splicing hotspot. Initial investigation in a cohort of tumor samples showed large variations in HER2 variant expression between patient samples. RNA interference studies identified 2 splicing factors involved in the regulation of splicing within this region, hnRNP H1 and SRSF3. siRNA targeting hnRNP H1 increases levels of X5 and the oncogenic variant ?16HER2. Furthermore RNA chromatography assays demonstrated binding of hnRNP H1 to RNA in this region. Additionally the proto-oncogene SRSF3 was also identified as an important regulator of splicing with SRSF3 knockdown resulting in changes in all the splice variants located at the hotspot. Most notably knockdown of SRSF3 resulted in a switch from the oncogenic ?16HER2 to p100 which inhibits cell proliferation. Binding of SRSF3 to RNA within this region was also demonstrated by RNA chromatography and more specifically 2 SRSF3 binding sites were identified within exon 15. SRSF3 and hnRNP H1 are the first splicing factors identified which regulate the production of these functionally distinct HER2 splice variants and therefore maybe important for the regulation of HER2 signaling.

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hnRNP L-RNA in HeLa

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2014-02-13 | E-GEOD-37562 | biostudies-arrayexpress