Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

P38-MAPK recruits the proteolysis pathways in Caenorhabditis elegans during bacterial infection

ABSTRACT: TiO2 column chromatography, MALDI-ToF-MS, SUMOylation, Coimmunoprecipitation and LC-MS/MS

INSTRUMENT(S): 6545 Q-TOF LC/MS

ORGANISM(S): Caenorhabditis Elegans

TISSUE(S): Whole Body

SUBMITTER: Krishnaswamy Balamurugan

LAB HEAD: Krishnaswamy Balamurugan

PROVIDER: PXD019172 | Pride | 2022-04-06

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

p38-MAPK recruits the proteolytic pathways in Caenorhabditis elegans during bacterial infection.

Balasubramaniam Boopathi B Vinitha Thondimuthu T Meenal Solai S VenkataKrishna Lappasi Mohanram LM Ravichandiran Velayutham V Balamurugan Krishnaswamy K

International journal of biological macromolecules 20220203

In eukaryotic organisms, cell-signalling completely relies on Post Translational Modifications (PTMs) that can function as regulatory switches. Phosphorylation is a fundamental and frequently occurring PTM in almost all eukaryotes. Herein, we have studied the importance of protein phosphorylation using classical proteomic techniques in C. elegans upon bacterial infection. The differentially regulated proteins during bacterial infection were excised from SDS-PAGE (One-Dimensional) gel (TiO<sub>2< ...[more]

PMID: 35124023

Similar Datasets

Podophyllum Hexandrum Royle MALDI-TOF-MS/MS

Project description:With the aim of reveal the mechanism of Podophyllum Hexandrum Royle adaption to high altitude, MALDI-TOF-MS/MS in combination with 2-DE was used to identify the differentially expressed proteins in leaves of Podophyllum Hexandrum Royle between low altitude (2200m) and high altitude (3100m), 65 differentially expressed proteins was identifed and 44 was up-regulated in high altitude compared tolow altitude.

2023-03-10 | PXD005640 | Pride

Podophyllum hexandrum Royle MS/MS

Project description:In order to study the molecular mechanisms of cold-adaption and PPT accumulation to understand why P. hexandrum adapts to chilling temperature, the differentially expressed proteins (DAPs) of P. hexandrum seedling exposed to chilling temperatures (4 and 10°C, 22°C as control) were conducted by using 2-DE in combination with MALDI-TOF-MS, a total of 35 DAP spots were detected and identified. Interestingly, 14 of the 35 DAPs played key roles in PPT biosynthesis, and 21 proteins participated in growth and development. These protein spots were classified into 7 functional categories, including PPT biosynthesis, primary metabolism, transcription and protein synthesis, cell growth/division, defense, transport, and energy. The present data would be useful in better understanding the molecular basis of chilling temperature response in P. hexandrum.

2017-05-15 | PXD003334 | Pride

Post-translational Regulation of FNIP1: a Rheostat for the Molecular Chaperone Hsp90

Project description:The molecular chaperone Hsp90 stabilizes and activates client proteins. Co-chaperones and post-translational modifications tightly regulate Hsp90 function and consequently lead to activation of clients. However, it is unclear whether this process occurs abruptly or gradually in the cellular context. We show that casein kinase-2 phosphorylation of the co-chaperone Folliculin-interacting protein-1 (FNIP1) on priming serine-938 and subsequent relay phosphorylation on serine-939, 941, 946, and 948 promotes its gradual interaction with Hsp90. This leads to incremental inhibition of Hsp90 ATPase activity and gradual activation of both kinase and non-kinase clients. We further demonstrate that serine/threonine protein phosphatase-5 (PP5) dephosphorylates FNIP1, allowing addition of O-GlcNAc (O-linked N-acetylglucosamine) to the priming serine-938. This process antagonizes phosphorylation of FNIP1, preventing its interaction with Hsp90, and consequently promotes FNIP1 lysine-1119 ubiquitination and proteasomal degradation. These findings provide a mechanism for gradual activation of the client proteins through intricate crosstalk of post-translational modifications of the co-chaperone FNIP1.

2019-01-31 | PXD012229 | Pride

Global proteomic analysis deciphers the mechanism of action of plant derived oleic acid against Candida albicans virulence and biofilm formation

Project description:Candida albicans is a commensal fungus in humans, mostly found on the mucosal surfaces of the mouth, gut, vagina and skin. Incidence of ever increasing invasive candidiasis in immunocompromised patients, alarming occurrence of antifungal resistance and insufficient diagnostic methods demand more focused research into C. albicans pathogenicity. Consequently, in the present study, oleic acid from Murraya koenigii was shown to have the efficacy to inhibit biofilm formation and virulence of Candida spp. Results of in vitro virulence assays and gene expression analysis, impelled to study the protein targets which are involved in the molecular pathways of C. albicans pathogenicity. Proteomic studies of differentially expressed proteins reveals that oleic acid induces oxidative stress responses and mainly targets the proteins involved in glucose metabolism, ergosterol biosynthesis, lipase production, iron homeostasis and amino acid biosynthesis. The current study emphasizes anti-virulent potential of oleic acid which can be used as a therapeutic agent to treat Candida infections.

2020-05-27 | PXD017588 | Pride

Extracellular vesicles of Acholeplasma laidlawii can be internalized by human fibroblasts and modulate expression of proteins

Project description:We demonstrated that extracellular vesicles of A. laidlawii can be internalized by human skin fibroblasts as a result of their co-incubation in vitro. Incubation of HSF with A. laidlawii EVs resulted in a significant modulation of 23 cellular proteins.

2022-02-17 | PXD027040 | Pride

Aeromonas hydrophila whole cell differential proteins

Project description:Differential protein of Aeromonas hydrophila(putative human infections)'s whole cell protein

2022-01-13 | PXD029702 | Pride

Enhancement of Tryptic Peptide Signals from Tissue Sections using MALDI IMS Post-ionization (MALDI-2)

Project description:Matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) allows for highly multiplexed, unlabeled mapping of analytes from tissue sections. However, further work is needed to improve sensitivity and depth of coverage for protein and peptide IMS. Laser-based post-ionization MALDI-2 has been shown to increase sensitivity for several molecular classes but has not yet been reported for peptides. We demonstrate signal enhancement of proteolytic peptides from thin tissue sections of human kidney by conventional MALDI (termed MALDI-1), and conventional MALDI augmented using a second ionizing laser (termed MALDI-2). Proteins were digested in situ using trypsin prior to IMS analysis. For tentative identification of peptides and proteins, a tissue homogenate from the same tissue analyzed by IMS was analyzed by LC-MS/MS. These proteins were digested in silico to generate a database of theoretical peptides to then match to MALDI IMS datasets. Peptides were tentatively identified by matching the MALDI peak list to the database peptide list employing a 5 ppm error window. This resulted in 314 ± 45 (n=3) peptides and 1 112 ± 84 (n=3) peptides for MALDI-1 and MALDI-2, respectively. Protein identifications requiring two or more peptides per protein resulted in 55 ± 13 proteins identifications with MALDI-1 and 205 ± 10 with MALDI-2. These results demonstrate that MALDI-2 provides enhanced sensitivity for the spatial mapping of tryptic peptides and significantly increases the number of proteins identified in IMS experiments.

2021-12-30 | PXD023877 | Pride

Global proteomic analysis of changes in the Caenorhabditis elegans proteome during Klebsiella pneumoniae infection

Project description:In this study, the changes in the global proteomics of C. elegans were analyzed by proteomics approach. The nematodes were exposed to K. pneumoniae for different time-points (12, 24 and 36 h) and the changes in the regulation were analyzed by employing mass spectrometry.

2017-09-06 | PXD007151 | Pride

Human salivary basic proline-rich proteins

Project description:Human basic proline-rich proteins and basic glycosylated proline-rich proteins are the most complex family of human adult salivary proteins, secreted only by the parotid gland, expressed by the polymorphic PRB1-4 genes. This study reports the results obtained for their characterization in our laboratory utilizing integrated top-down and bottom-up HPLC-ESI-MS and MS/MS platform. The family include 11 parent peptides/proteins and more than 6 parent glycosylated proteins. Despite the complexity, on the basis of their primary structure they result the product of the duplication of three repeats and we propose that they can be classified in two main groups, the first including the peptides called P-E, P-Ko, IB-6, Ps-1, Ps-2, P-H, P-F, P-J, and P-D, the second including the peptides called IB-1, II-2 and the glycosylated basic proline-rich proteins codified by PRB3 and PRB4 genes. A third minor hybrid group includes the proteins called IB-8a Con1- and Con1+. Some of the proteins of the family (IB-1, II-2 and P-J) are almost always detectable in adult human saliva, while the others are expressed with different frequencies according to the phenotype. Various isoforms are detectable in the adult saliva and three of them, until now not reported (P-H S1→A, P-Ko P36→S, P-Ko A41→S), were characterized by MS/MS fragmentation.

2018-08-08 | PXD009813 | Pride

Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins

Project description:The aim of the MS analysis is to identify fatty acids modifying Cys3 of GNAI3. Detailed description in the manuscript Nuskova et al. submitted to NatComms.

2021-07-22 | PXD021517 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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