Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Spironucleus salmonicida endocytic interactors

ABSTRACT: We probed interactors of S. salmonicida CHC interactors by the means of native co-IP.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Spironucleus Salmonicida

SUBMITTER: Rui Santos

LAB HEAD: Prof. Adrian Hehl

PROVIDER: PXD020201 | Pride | 2022-04-14

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20191217_rs_12881_Ss_CHC_1.raw	Raw
	20191217_rs_12881_Ss_CHC_1F283542.mzid.gz	Mzid
	20191217_rs_12881_Ss_CHC_1F283542.mzid_20191217_rs_12881_Ss_CHC_1_F283542.MGF	Mzid
	20191217_rs_12881_Ss_CHC_2.raw	Raw
	20191217_rs_12881_Ss_CHC_2F283543.mzid.gz	Mzid

Items per page:

1 - 5 of 48

Similar Datasets

The interactomes of GlPXD2 and 4 PIP-binding proteins in Giardia lamblia

Project description:We investigated the composition of the interactomes of overall 7 proteins in the parasitic protist Giardia lamblia, some of which were found to be associated to clathrin assemblies. This accession refers to proteins GlPXD2 and 4

2019-05-20 | PXD013899 | Pride

The interactomes of GlPXD1, 3 and 6 PIP-binding proteins in Giardia lamblia

Project description:We investigated the composition of the interactomes of 7 proteins in the parasitic protist Giardia lamblia, some of which were found to be associated to clathrin assemblies. This accession refers to the first three namely GlPXD1, 3 and 6.

2019-05-20 | PXD013890 | Pride

The interactomes of GlFYVE PIP-binding protein in Giardia lamblia

2019-05-20 | PXD013897 | Pride

The interactomes of GlNECAP PIP-binding proteins in Giardia lamblia

2019-05-20 | PXD013896 | Pride

Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation

Project description:Serine residues in the charged linker region of human Hsp90beta are highly phoshporylated in vivo. Mutation of these residues to alanines resulted in altered binding of many Hsp90beta interactors. This project contains the data and searches related to co-immunoprecipitation experiments with wild-type and mutant Hsp90beta, as well as input.

2021-07-07 | PXD025873 | Pride

ChIP-Seq sequencing of novel interactors of H3K4me3, H3K36me3 and H3K9me3

Project description:This study describes the epigenetic profiling of the novel interactors of H3K4me3, H3K36me3 or H3K9me3. The interactors were ChIP-Seq profiled by their GFP tag in stably transfected HeLa (Kyoto) cells. The interactors include GATAD1, Sgf29, BAP18, TRRAP, PHF8, N-PAC and LRWD1 (including replicates), as well as an GFP ChIP-Seq profile on non-transfected HeLa cells (negative control). Also included are the profiles of the histone modifications themselves (H3K4me3, H3K27me3, H3K9me3, H3K36me3, H3K9/14Ac and H3K79me3) ChIP-Seq profiling of 8 proteins by their GFP tag in stably transfected cells HeLa (Kyoto) cells, 6 replicas, as well as ChIP-Seq profiling of 6 histone modifications in wt HeLa (Kyoto) cells

2010-09-17 | E-GEOD-20303 | biostudies-arrayexpress

ESCRT complexes in Giardia intestinalis (CHMP7)

Project description:To access ESCRT subunit presence, distribution and main interactors, we performed iterative co-immunoprecipitation on recombinant Giardia subunits.

2021-04-10 | PXD016487 | Pride

Identification of Snf2L-associated chromatin remodeling complex subunits in Plasmodium falciparum

Project description:ATP-dependent chromatin remodeling enzymes re-position and evict nucleosomes at specific genomic loci and therefore are essential regulators of all DNA dependent processes. They act in the context of large multiprotein complexes. The malaria-causing parasite Plasmodium falciparum (Pf) possesses a reduced set of chromatin remodeling enzymes, which are highly divergent, and no associated complex subunits are known. Within a detailed characterization of the ISWI-type remodeler PfSnf2L (PF3D7_1104200), potential interactors were identified. The protein was tagged endogenously in the parasite and co-immunoprecipitated. Subsequent LC-MS/MS analysis provided a list of specific protein interactors with a strong link to chromatin organization including nucleosome assembly factors, transcription factors as well as Plasmodium-specific uncharacterized proteins. The results suggest a functional role of PfSnf2L in nucleosome assembly and transcription regulation and point towards novel Plasmodium-specific chromatin remodeling complexes.

2024-10-17 | PXD041155 | Pride

Adult mouse choroid plexus OTX2 Co-IP

Project description:To analyze OTX2 function in adult choroid plexus, we performed several OTX2 co-immunoprecipitation (co-IP) experiments with mass spectrometry analysis to identify potential protein partners. We previously discovered that OTX2 protein also accumulates non-cell autonomously in subventricular zone (SVZ) and rostral migratory stream (RMS) astrocytes and in visual cortex (VCx) parvalbumin cells. The identification of alternate protein partners in cell-autonomous and non-cell-autonomous contexts would suggest OTX2 takes on specific roles after transferring between cells. In order to test this hypothesis, and to reinforce choroid plexus analysis, we also performed OTX2 co-IP on lysates from adult mouse SVZ, RMS and VCx.

2021-08-23 | PXD021244 | Pride

TAPL interaction network - Lysosomal targeting of the ABC transporter TAPL is determined by membrane localized charged residues

Project description:The human lysosomal polypeptide ABC transporter TAPL (ABC subfamily B member 9, ABCB9) transports 6–59 amino-acids-long polypeptides from the cytosol into lysosomes. The subcellular localization of TAPL depends solely on its N-terminal transmembrane domain TMD0, which lacks conventional targeting sequences. However, the intracellular route and the molecular mechanisms that control TAPL localization remain unclear. Here, we delineated the route of TAPL to lysosomes and investigated the determinants of single trafficking steps. By synchronizing trafficking events by retention using selective hooks (RUSH) assay and visualizing individual intermediate steps through immunostaining and confocal microscopy, we demonstrate that TAPL takes the direct route to lysosomes. We further identified conserved charged residues within TMD0 transmembrane helices that are essential for individual steps of lysosomal targeting. Substitutions of these residues retained TAPL in the endoplasmic reticulum (ER) or Golgi. We also observed that for release from the ER, a salt bridge between Asp-17 and Arg-57 is essential. An interactome analysis revealed that Yip1-interacting factor homolog B, membrane-trafficking protein (YIF1B) interacts with TAPL. We also found that YIF1B is involved in ER-to-Golgi trafficking and interacts with TMD0 of TAPL via its transmembrane domain and that this interaction strongly depends on the newly identified salt bridge within TMD0. These results expand our knowledge about lysosomal trafficking of TAPL and the general function of extra transmembrane domains of ABC transporters.

2019-03-14 | PXD010989 | Pride

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