Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Immunoprecipitaiton of Rab27a from mouse melanoma cells

ABSTRACT: To identify the co-immunoprecipitating proteins of Rab27a following Rab27a pull down of B16-F1 mouse melanoma cells infected with adenovirus expressing GFP-hsSPIRE1.

INSTRUMENT(S): TripleTOF 6600

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Melanocyte, Cell Culture

DISEASE(S): Melanoma

SUBMITTER: Amanda Miles

LAB HEAD: Amanda Miles

PROVIDER: PXD018083 | Pride | 2020-05-15

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	191129_Alastair_UoN_GFP_Sp1_IDA_i1.wiff	Wiff
	191129_Alastair_UoN_GFP_Sp1_IDA_i1.wiff.scan	Wiff
	191129_Alastair_UoN_GFP_Sp1_IDA_i1i2i3.group	Other
	191129_Alastair_UoN_GFP_Sp1_IDA_i2.wiff	Wiff
	191129_Alastair_UoN_GFP_Sp1_IDA_i2.wiff.scan	Wiff

Items per page:

1 - 5 of 7

Publications

Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins.

Alzahofi Noura N Welz Tobias T Robinson Christopher L CL Page Emma L EL Briggs Deborah A DA Stainthorp Amy K AK Reekes James J Elbe David A DA Straub Felix F Kallemeijn Wouter W WW Tate Edward W EW Goff Philip S PS Sviderskaya Elena V EV Cantero Marta M Montoliu Lluis L Nedelec Francois F Miles Amanda K AK Bailly Maryse M Kerkhoff Eugen E Hume Alistair N AN

Nature communications 20200713 1

Cell biologists generally consider that microtubules and actin play complementary roles in long- and short-distance transport in animal cells. On the contrary, using melanosomes of melanocytes as a model, we recently discovered that the motor protein myosin-Va works with dynamic actin tracks to drive long-range organelle dispersion in opposition to microtubules. This suggests that in animals, as in yeast and plants, myosin/actin can drive long-range transport. Here, we show that the SPIRE-type a ...[more]

PMID: 32661310

Similar Datasets

Protein profiling of stress-activated breast cancer cell models

Project description:This study provides insights into the efficacy of beta-blockers as breast cancer therapeutics.Cell line models of basal-type and estrogen receptor-positive breast cancer were profiled for basal levels of adrenoceptor gene/protein expression, and ADRβ2-mediated cell behaviour including migration, invasion, adhesion, and proliferation in response to adrenoceptor agonist/antagonist treatment. Protein profiling and histology identified response biomarkers and drug targets. Protein profiling revealed the upregulation of the pro-metastatic gene LYPD3 in norepinephrine treated MDA MB 468 cells. Histology confirmed selective LYPD3 expression in clinical primary and metastatic breast tumours. These findings demonstrate that basal-type cancer models show a more aggressive ADRβ2-activated phenotype in the resting and stimulated state, which is attenuated by ADRβ2 inhibition, and explain some of the previous studies that have cast doubt on the value of beta-blocker therapy in breast cancer. These findings suggest that propranolol should be clinically evaluated in patients with basal-type tumours expressing high levels of ADRβ2 and LYPD3.

2020-05-26 | PXD009488 | Pride

Shotgun proteomic profiling of intestinal mucosa of rainbow trout Oncorhynchus mykiss

Project description:The objective of this study was to identify and quantify proteomic profiles of intestine of rainbow trout (Oncorhynchus mykiss). Specific pathogen free rainbow trout (mean length 15 ± 1 cm) were maintained in recirculating de-chlorinated water at 19±1 °C. Prior to the experiment, fish were distributed between aquaria. The test groups were infected by immersion of Yersinia ruckeri CSF007-82 (biotype 1) and 7959-11 (biotype 2) strains. The control group was immersed similar with sterile broth medium. Fish were anaesthetized and sampled aseptically at different time points. Each intestine was washed three times with sterile phosphate-buffered saline containing a cocktail of mammalian protease inhibitors. Intestinal mucosa was scraped with a sterile large scalpel blade. Intestinal samples were snap-frozen in liquid nitrogen and stored at –80 °C.

2019-11-12 | PXD011087 | Pride

Molecular characterization of Histomonas meleagridis exoproteome with emphasis on protease secretion and parasite-bacteria interaction - SWATH dataset

Project description:Exoproteome from parasitic protists constitutes of extracellular proteins which play a fundamental role in multifactorial host-parasite interactions. Lytic factors, especially secreted proteases in extracellular milieu, are capable to modulate tissue invasion, thereby aggravating host susceptibility. Despite the important role of exoproteins during infection, exoproteomic data on Histomonas meleagridis are non-existent. The present study employed traditional 1D-in-gel-zymography (1D-IGZ) and micro-LC-ESI-MS/MS (shotgun proteomics), to scrutinize H. meleagridis exoproteomes, obtained from a clonal virulent and attenuated strains. Both strains were maintained as mono-eukaryotic monoxenic culture with Escherichia coli. We demonstrated active in vitro secretion kinetics of proteases by both parasites, with widespread proteolytic activity ranging from 17 kDa to 120 kDa. Based on protease inhibitor-susceptibility tests, a predominant repertoire of cysteine proteolysis was present in the parasite exoproteomes, with stronger activity from virulent H. meleagridis. Shotgun proteomics, aided by customized database, identified 176 proteins including actin, potential moonlighting glycolytic enzymes, lytic molecules such as pore-forming proteins (PFPs) and proteases like cathepsin-L like cysteine protease. To quantify the exoproteomic differences between the virulent and the attenuated H. meleagridis cultures, a sequential window acquisition of all theoretical spectra mass spectrometric (SWATH-MS) approach was applied. Surprisingly results showed most of the exoproteomic differences to be of bacterial origin, involving metabolism and locomotion. By deciphering such molecular signatures, novel insights into an inherent complex in vitro protozoan- bacteria relationship was elucidated.

2019-02-11 | PXD012038 | Pride

Reanalysis of PXD012038: "Molecular characterization of Histomonas meleagridis exoproteome with emphasis on protease secretion and parasite-bacteria interaction - SWATH dataset"

2023-03-11 | PXD034834 | Pride

Shotgun proteomic profiling of spleen of rainbow trout Oncorhynchus mykiss

Project description:The objective of this study was to identify and quantify proteomic profiles of spleen of rainbow trout Oncorhynchus mykiss. Specific pathogen free rainbow trout (mean length 15 ± 1 cm) were maintained in recirculating de-chlorinated water at 19±1 °C. Prior to the experiment, fish were distributed between 9 aquaria, 18 fish per aquarium. The test groups were infected by immersion of Yersinia ruckeri strains: CSF007-82 (biotype 1) and 7959-11 (biotype 2). The control group was immersed similar with sterile broth medium. There were 3 aquaria per each group (CSF007-82-infected, 7959-11-infected and control). Nine fish from infected and control fish groups were anaesthetized with MS-222 at 3, 9 and 28 days post exposure and sampled aseptically. Each spleen was washed three times with sterile phosphate-buffered saline containing a cocktail of mammalian protease inhibitors. Spleen samples were snap-frozen in liquid nitrogen and stored at –80 °C.

2018-08-14 | PXD008478 | Pride

Shotgun proteomic profiling of head kidney of rainbow trout Oncorhynchus mykiss

Project description:The objective of this study was to identify and quantify proteomic profiles of head kidney of rainbow trout Oncorhynchus mykiss. Specific pathogen free rainbow trout (mean length 15 ± 1 cm) were maintained in recirculating de-chlorinated water at 19±1 °C. Prior to the experiment, fish were distributed between 9 aquaria, 18 fish per aquarium. The test groups were infected by immersion of Yersinia ruckeri strains: CSF007-82 (biotype 1) and 7959-11 (biotype 2). The control group was immersed similar with sterile broth medium. There were 3 aquaria per each group (CSF007-82-infected, 7959-11-infected and control). Nine fish from infected and control fish groups were anaesthetized with MS-222 at 3, 9 and 28 days post exposure and sampled aseptically. Each head kidney was washed three times with sterile phosphate-buffered saline containing a cocktail of mammalian protease inhibitors. Head kidney samples were snap-frozen in liquid nitrogen and stored at –80 °C.

2018-08-14 | PXD008473 | Pride

Mildly pathogenic Rickettsia-macrophage interactions

Project description:The molecular details underlying differences in pathogenicity between Rickettsia species remain to be fully understood. Evidence points to macrophage permissiveness as a key mechanism in rickettsial virulence. Different studies have shown that several rickettsial species responsible for mild forms of rickettsioses can also escape macrophage-mediated killing mechanisms and establish a replicative niche within these cells. However, their manipulative capacity with respect to host cellular processes is far from being understood. A deeper understanding of the interplay between mildly pathogenic rickettsiae and macrophages and the commonalities and specificities of host responses to infection would illuminate differences in immune evasion mechanisms and pathogenicity. We have used quantitative proteomics by SWATH-MS/MS to profile alterations resulting from infection of THP-1 macrophages with three mildly pathogenic rickettsiae: R. parkeri, R. africae, and R. massiliae, all successfully proliferating in these cells. We show that all three species trigger different proteome signatures. Our results reveal a significant impact of infection in proteins categorized as type-I interferon responses, here included several components of the RIG-1-like signaling pathway, mRNA splicing, and protein translation. Moreover, significant differences in protein content between infection conditions anticipate species-specific induced alterations. Indeed, we confirm a distinct impact on host inflammatory responses between species during infection, demonstrating that these species trigger different levels of INF-β, differences in the bioavailability of the pro-inflammatory cytokine IL1-β, and in triggering pyroptotic events. This work reveals novel aspects and exciting nuances of macrophage-Rickettsia interactions, adding additional layers of complexity between Rickettsia and host cells constant arms race for survival.

2022-01-11 | PXD026982 | Pride

Quantitative chemical proteomics of Leishmania mexicana

Project description:We report the first systematic study of the effect of Hsp90 inhibition on the global protein synthesis in Leishmania parasites using an integrated chemical biology approach. Heat shock protein 90 (Hsp90) is a conserved molecular chaperone responsible for the folding of newly synthesised proteins. It is regarded as a master regulator of protein homeostasis of the cell, and its inhibition has been proposed to affect functions of a large array of its client proteins. We showed that the Hsp90 inhibition affects synthesis of many Leishmania proteins, with important chaperones and virulence factors showing an overall increased relative expression whilst many ribosomal proteins showing a down-regulation. This study defines the Leishmania parasite’s response to Hsp90 inhibition at its nascent global protein synthesis and provides a rich resource for future studies on Leishmania biology and antileishmanial drug development.

2021-04-23 | PXD022708 | Pride

Quantitative proteomics of Hsp90 inhibition in Leishmania mexicana

Project description:Using a combination of mass spectrometry-based quantitative proteomics, chemical and metabolic labelling, we provide the first protein-level evidence that the Hsp90 inhibition affects the expression of hundreds of proteins in Leishmania spp. Our study defines the Leishmania parasite’s response to Hsp90 inhibition at its global proteome and provides a rich resource for future studies on Leishmania biology and antileishmanial drug development.

2021-04-23 | PXD024764 | Pride

Starvation-specific NSPs in Leishmania mexicana parasites by quantitative proteomics

Project description:Using a combination of BONCAT technique and iTRAQ 3-plex quantitative proteomics MS, we profiled the de novo protein synthesis in the starving L. mexicana parasites in a temporally resolved manner. This approach uniquely integrates the high specificity of the BONCAT technique for the NSPs with the high sensitivity and multiplexed quantitation capability of the iTRAQ quantitative proteomics MS. Proof-of-concept experiments identified over 250 starvation-specific NSPs in the parasite and quantified the relative changes in abundance of these proteins as a function of duration of starvation.

2019-12-04 | PXD015827 | 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