Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MRNA targeting to the human ER

ABSTRACT: Besides targeting of precursor polypeptides to the human endoplasmic reticulum (ER), mRNAs are targeted to the ER. While the first targeting process is reansonably well understood, relatively little is known about the latter. To obtain novel insights into mRNA targeting to the human ER, we combined siRNA-mediated depletion of putative mRNA-receptors of the ER-membrane in HeLa cells with label-free quantitative proteomics and differential expression analysis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Richard Zimmermann

LAB HEAD: Prof. Dr. Richard Zimmermann

PROVIDER: PXD011990 | Pride | 2021-06-14

REPOSITORIES: pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20160826_coreQEP1_NaNa_QC_Orbi2314Sample01.raw	Raw
	20160826_coreQEP1_NaNa_QC_Orbi2314Sample02.raw	Raw
	20160826_coreQEP1_NaNa_QC_Orbi2314Sample03.raw	Raw
	20160826_coreQEP1_NaNa_QC_Orbi2314Sample04.raw	Raw
	20160826_coreQEP1_NaNa_QC_Orbi2314Sample05.raw	Raw

Items per page:

1 - 5 of 16

Similar Datasets

mRNA targeting to the human ER

Project description:Besides nascent and fully synthesized precursor polypeptides, mRNAs are targeted to the human endoplasmic reticulum (ER). In contrast to precursor targeting, however, little is known about mRNA targeting. To gain novel insights into the latter process, we combined siRNA-mediated depletion of putative ER-membrane resident mRNA- receptors in HeLa cells with label-free quantitative proteomics and differential expression analysis.

2021-06-14 | PXD011989 | Pride

Targeting of precursor polypeptides to the human ER

Project description:Various pathways can target nascent or fully synthesized precursor polypeptides to the human endoplasmic reticulum (ER). Typically, they involve cytosolic proteins or complexes and their respective receptors on the ER surface. The signal recognition particle (SRP) and the heterodimeric SRP-receptor (SR) represent one such targeting system, others are TRC40 and its heterodimeric TRC-receptor (WRB/CAML) and the components of the SND pathway. Apparently, they all can target precursor polypeptides to the Sec61-channel in the ER membrane. To characterize the substrate specificities of these targeting pathways, we combined siRNA-mediated depletion of membrane receptor subunits in HeLa cells with label-free quantitative proteomics and differential protein abundance analyis.

2020-03-06 | PXD011993 | Pride

Polypeptide targeting to distinct areas of the human ER

Project description:There is at least one additional targeting pathway for proteins to the human endoplasmic reticulum, which involves a cytosolic as well as an ER-membrane resident receptor, belonging to the family of PEX proteins. In contrast to the precursor protein targeting pathways, the additional pathway targets proteins to distinct ER sites and does not target proteins to the Sec61 complex. To characterize substrate proteins of this pathway, we combined siRNA-mediated PEX3-depletion in HeLa cells with label-free quantitative proteomics and and differential protein abundance analysis.

2021-12-20 | PXD012005 | Pride

Substrates of human Sec62/Sec63 complex

Project description:The Sec61-associated Sec62/Sec63 complex supports translocation of only a subset of precursor polypeptides, i.e. in a substrate-specific manner. To characterize Sec62/Sec63-dependent precursors, we combined siRNA-mediated Sec62 or Sec63 depletion in Hela cells or CRISPR/Cas9-mediated knock-down in HEK 293 cells with label-free quantitative proteomics and differential expression analysis.

2020-03-06 | PXD012078 | Pride

siRNAs 15-29 nucleotides long with 100 percent hit to Cocksfoot streak virus

Project description:Cocksfoot grass (Dactylis glomerata) collected from Wytham, Oxford, UK, was tested for Cocksfoot streak virus infection. Small RNA of the grass was extracted and converted to DNA according to Ho, T., et al. (2008) Biochem Biophys Res Commun. 368:433-7, with primers modified to contain 454 adapter nucleotide sequences. The DNA then passed quality control through Bioanalyzer and Nanodrop before sequenced by 454 Life Sciences. Keywords: siRNA One sample analyzed by 454 high-throughput sequencing technology

2008-09-11 | E-GEOD-12052 | biostudies-arrayexpress

Cotranslational signal independent SRP preloading during membrane targeting

Project description:Cotranslational targeting into the endoplasmic reticulum (ER) by the Signal Recognition Particle (SRP) is a key event determining polypeptide fate in eukaryotic cells. Here, we globally define the principles and mechanisms of SRP binding and ER targeting in vivo. Cotranslational targeting through SRP is the dominant route into the ER for all secretory proteins, regardless of targeting signal characteristics. Cytosolic SRP functions in a pioneer translation round that builds a membrane-resident mRNAs pool, explaining how low SRP levels suffice for the secretory load. SRP does not induce an elongation arrest; consequently, kinetic competition between targeting and translation elongation dictates which substrates are translocated post-translationally. Unexpectedly, SRP binds most secretory ribosomal complexes before targeting signals are synthesized. We show non-coding mRNA elements can promote signal-independent SRP pre-recruitment. Our study defines the complex kinetic interplay between elongation and determinants in the polypeptide and mRNA modulating SRP-substrate selection and membrane targeting in vivo. Ribosome profiling (RiboSeq) and RNA-seq of subcellular fractions of ribosomes. Soluble and membrane bound ribosomes are separated by centrifugation, and SRP-bound ribosomes are immunoprecipitated from the soluble fraction. Polysomes and monosomes are separated by sucrose gradient ultracentrifugation.

2016-08-03 | E-GEOD-74393 | biostudies-arrayexpress

Cotranslational signal independent SRP preloading during membrane targeting

2016-08-03 | GSE74393 | GEO

T Cell Receptor Based Therapy of Metastatic Colorectal Cancer

Project description:T Cell Receptor Based Therapy of Metastatic Colorectal Cancer With mRNA-engineered T Cells Targeting Transforming Growth Factor Beta Receptor Type II (TGFβII)

| 2265728 | ecrin-mdr-crc

Release of a nuclear ubiquitin-like protein activates proteasomal degradation of mislocalized hydrophobic mitochondrial proteins in trypanosomes

Project description:Mitochondrial protein import in the parasitic protozoan Trypanosoma brucei is mediated by the atypical outer membrane translocase, ATOM. It consists of seven subunits including ATOM69, the import receptor for hydrophobic proteins. Ablation of ATOM69, but not of any other subunit, triggers a unique quality control pathway resulting in the proteasomal degradation of non-imported mitochondrial proteins. The process requires a protein of unknown function, an E3 ubiquitin ligase and the ubiquitin-like protein (TbUbL1), which all are recruited to the mitochondrion upon ATOM69 depletion. TbUbL1 is a nuclear protein, a fraction of which is released to the cytosol upon triggering of the pathway. Nuclear release is essential since cytosolic TbUbL1 can bind mislocalized mitochondrial proteins and likely transfers them to the proteasome. Mitochondrial quality control has previously been studied in yeast and metazoans. Finding such a pathway in the highly diverged trypanosomes suggests such pathways are an obligate feature of all mitochondria.

2022-05-04 | PXD027739 | Pride

Estrogen-induced lncRNA, LINC02568, promotes estrogen receptor-positive breast cancer development and drug resistance through both in trans- and in cis-mechanisms

Project description:Estrogen and estrogen receptor (ER) signaling play critical roles in the development of ER-positive breast cancer, and endocrine therapy is the frontline treatment for ER-positive breast cancer patients. However, the primary and acquired resistance to endocrine therapy including tamoxifen and fulvestrant remains as the major challenge in the clinic. Here, we identified an estrogen-induced lncRNA, LINC02568, through transcriptomic analysis, which is highly expressed in ER-positive breast cancer. LINC02568 is functional important in ER-positive breast cancer cell growth in vitro and tumorigenesis in vivo as well as endocrine therapy resistance. Mechanically, we demonstrated that LINC02568 regulates, in trans, estrogen/ERα-induced gene transcriptional activation by sponging miR-1233-5p to stabilize ESR1 mRNA in the cytoplasm. Meanwhile, LINC02568 contributes to tumor-specific pH homeostasis in breast cancer cells by regulating CA12 in cis in the nucleus. The dual functions of LINC02568 together contribute to breast cancer cell growth and tumorigenesis as well as endocrine therapy resistance. Antisense oligonucleotides (ASO) targeting LINC02568 significantly inhibits ER-positive breast cancer cell growth in vitro and tumorigenesis in vivo as well as resensitize tamoxifen-resistant cells to tamoxifen. Furthermore, combination treatment with ASO targeting LINC02568 and tamoxifen exhibits synergistic effect on tumor growth. Taken together, our findings revealed dual mechanisms of LINC02568 in regulating ERα signaling and pH homeostasis in ER-positive breast cancer, and indicated that targeting LINC02568 might represent a potential therapeutic avenue in clinic.

2023-09-13 | GSE217190 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data