Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Comparative proteomic identification of Rab GTPase interactors in Arabidopsis

ABSTRACT: Rab GTPases are key spatio-temporal regulators of endomembrane trafficking and endomembrane compartment identity across eukaryotes. This therefore makes them ideal targets for study of endomembrane compartment and trafficking pathway composition. In plants, few definitive interactors of Rab GTPases and cargoes of their associated trafficking pathways are known, hindering our understanding of how plants may accomplish and support some unique aspects and requirements of their post-Golgi trafficking systems. The purpose of this work was to identify candidate interactors of different post-Golgi Rab GTPases in Arabidopsis. Co-IPs were performed against tagged-versions of three different post-Golgi Rab GTPases: RAB-A5c, RAB-A2a and RAB-G3f, as well as against control wild-type (Col-0) plants. Comparative ranking of the different proteomes produced candidate interactor lists enriched in possible specific interactors of each Rab GTPase, as well as generic shared interactors. This dataset forms the basis of the characterisation work of several upcoming publications.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Root

SUBMITTER: Liam Elliott

LAB HEAD: Charlotte Kirchhelle

PROVIDER: PXD044263 | Pride | 2023-09-21

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Rab30 regulates lipid homeostasis in the hepatocyte during fasting

Project description:In order to facilitate inter-tissue communication and exchange of proteins, lipoproteins, and metabolites with the circulation, hepatocytes have an intricate and efficient intracellular trafficking system regulated by small Rab GTPases. Rab30, a putative Golgi-localized Rab GTPase, is induced in the mouse liver by fasting and its expression is further amplified in liver-specific carnitine palmitoyltransferase 2 knockout mice (Cpt2L-/-) that lack the ability to oxidize fatty acids in a Pparα-dependent manner. Live-cell super-resolution imaging and biochemical in vivo proximity labeling demonstrated that Rab30-marked vesicles are highly dynamic and interact with proteins throughout the secretory pathway. Rab30 whole-body, liver-specific, and Rab30;Cpt2 liver-specific double knockout (DKO) mice are viable and display intact Golgi ultrastructure. However, the loss of Rab30 in Rab30;Cpt2 DKO mice suppresses serum dyslipidemia observed in Cpt2L-/- single knockout mice. Corresponding with decreased serum triglyceride and cholesterol levels, Rab30;Cpt2 DKO mice exhibit decreased circulating but not hepatic ApoA4 protein, indicative of a trafficking defect. Together, these data suggest a role for Rab30 in the selective sorting of lipoproteins to influence hepatocyte and circulating triglyceride levels particularly during times of excessive lipid burden

2023-09-12 | GSE240396 | GEO

Effect of Rinl deficiency on ex vivo isolated naïve and effector/memory CD4+ T cells

Project description:Rab GTPases are primarly involved in trafficking processes. Rinl belongs to the Ras-interaction/interference (Rin) proteins and is a guanine nucleotide exchange factor (GEF) for Rab5a and Rab22. By transcriptome analysis of naïve and effector CD4+ T cells we identify Rinl-regulated pathways in CD4+ T cells.

2023-08-28 | GSE235805 | GEO

Comparison of expression data between control and Ovo1 morphant zebrafish embryos

Project description:A fundamental issue in cell biology is how migratory cell behaviors are controlled by dynamically regulated cell adhesion. Vertebrate neural crest (NC) cells rapidly alter cadherin expression and localization at the cell surface during migration. Secreted Wnts induce some of these changes in NC adhesion and also promote specification of NC-derived pigment cells. Here, we show that the zebrafish transcription factor Ovo1 is a Wnt target gene that controls migration of pigment precursors by regulating the intracellular movements of N-cadherin (Ncad). Ovo1 genetically interacts with Ncad and its depletion causes Ncad to accumulate inside cells. Ovo1-deficient embryos strongly upregulate factors involved in intracellular trafficking, including several rab GTPases, known to modulate cellular localization of cadherins. Surprisingly, NC cells express high levels of many of these rab genes in the early embryo, chemical inhibitors of Rab functions rescue NC development in Ovo1-deficient embryos and overexpression of a Rab-interacting protein leads to similar defects in NC migration. These results suggest that Ovo proteins link Wnt signaling to intracellular trafficking pathways that localize Ncad in NC cells and allow them to migrate. Similar processes probably occur in other cell types in which Wnt signaling promotes migration.

2010-04-28 | GSE21539 | GEO

Comparison of expression data between control and Ovo1 morphant zebrafish embryos

2010-04-27 | E-GEOD-21539 | biostudies-arrayexpress

Expression data from control and Ascorbic Acid (AA) stimulated Mc-3T3-E1 osteoblasts

Project description:Despite advances in investigating functional aspects of osteoblast (OB) differentiation, especially studies on how bone proteins are deposited and mineralized, there has been little research on the intracellular trafficking of bone proteins during OB differentiation. Collagen synthesis and secretion is markedly upregulated upon Ascorbic Acid (AA) stimulation. Understanding the mechanism by which collagen is mobilized in specialized OB cells is important for both basic cell biology and diseases involving defects in bone secretion and deposition. RabGTPases are major regulators on protein trafficking throughout the cell. In this study, we identified the Rab GTPases that are upregulated during 5-day AA differentiation of OBs using microarray analysis, namely Rab1, Rab3d and Rab27b. We used microarrays to detail the global programme of gene expression underlying procollagen production and trafficking and identified up-regulated genes during this process. Control Mc3T3-E1 cells and 5 day Ascorbic Acid stimulated cells were processed for RNA extraction and hybridization on Affymetrix microarrays.

2012-05-01 | E-GEOD-37676 | biostudies-arrayexpress

Expression data from control and Ascorbic Acid (AA) stimulated Mc-3T3-E1 osteoblasts

2012-05-02 | GSE37676 | GEO

Rab30 regulates lipid homeostasis in the hepatocyte during fasting

2024-05-04 | PXD050376 | Pride

Rab30 regulates lipid homeostasis in the hepatocyte during fasting

2023-09-12 | PXD044528 | Pride

Detection of structure-specific interactions of Rab GTPases

Project description:Protein–protein interactions (PPIs) mediate multiple essential functions and regulatory events in living organisms. The physical interactome of a given protein can be abnormally altered in response to external and internal cues, thus modulating cell physiology and contributing to human pathologies including neurodegenerative diseases. Despite substantial efforts, current approaches cannot pinpoint structure-specific PPIs or their interaction interfaces on a proteome-wide scale. To address this limitation, we have adapted the structural proteomics method known as limited proteolysis–mass spectrometry to identify PPIs by probing protein structural alterations within cellular extracts upon treatment with a protein of interest. Here, we added Rab GTPases, namely Rab5A and Rab2A in their GTP- and GDP-bound forms to a HEK293T cellular extract and probed their structure-specific interactomes. We identified already know interactors of these proteins bassed on previously published data as well as a number of candidate interactor proteins.

2024-02-10 | PXD048849 | Pride

PPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins

Project description:Mutations that activate LRRK2 protein kinase cause Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases within their Switch-II motif controlling interaction with effectors. An siRNA screen of all protein phosphatases revealed that a poorly studied protein phosphatase, PPM1H, counteracts LRRK2 signaling by specifically dephosphorylating Rab proteins. PPM1H knock out increased endogenous Rab phosphorylation and inhibited Rab dephosphorylation. Overexpression of PPM1H suppressed LRRK2-mediated Rab phosphorylation. PPM1H also efficiently and directly dephosphorylated Rab8A in biochemical studies. A “substrate-trapping” PPM1H mutant (Asp288Ala) binds with high affinity to endogenous, LRRK2-phosphorylated Rab proteins, thereby blocking dephosphorylation seen upon addition of LRRK2 inhibitors. PPM1H is localized to the Golgi and its knockdown suppresses primary cilia formation, similar to pathogenic LRRK2. Thus, PPM1H acts as a key modulator of LRRK2 signaling by controlling dephosphorylation of Rab proteins. PPM1H activity enhancers could offer a new therapeutic approach to prevent or treat Parkinson’s disease

2019-11-06 | PXD014794 | 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