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ProteomicsDown-regulation of Rab 5C-dependent Endocytosis and Glycolysis in Cisplatin-resistant Ovarian Cancer Cell Lines
Drug resistance poses a major challenge to ovarian cancer treatment. Understanding mechanisms of drug resistance is important for finding new therapeutic targets. In the present work, a cisplatin-resistant ovarian cancer cell line A2780-DR was established with a resistance index of 6.64. The cellula...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080724 | MassIVE
ProteomicsRAB GTPase proximity interactome
RAB GTPases represent the most abundant family of small GTPases and regulate multiple aspects of membrane trafficking events, from cargo sorting to vesicle budding, transport, docking, and fusion. To control these processes, RABs are tightly regulated by guanine exchange factors (GEFs) and GTPase-ac...
ORGANISM(S): Homo sapiens (Human) 
2025-12-02 | PXD057404 | Pride
Rab gtpase Apex2 Membrane trafficking Bioid 
ProteomicsInteractions between Transport Protein Particle (TRAPP) complexes and Rab GTPases in Arabidopsis
The Transport Protein Particle II (TRAPPII) is essential for exocytosis, endocytosis, protein sorting and cytokinesis. In spite of a considerable understanding of its biological role, little is known about Arabidopsis TRAPPII complex topology and molecular function. In this study, independent proteo...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-09-03 | PXD013016 | Pride
Trappii Arabidopsis Co-ip Protein complex Rab gtpases Transport protein particle 
ProteomicsComparative proteomic identification of Rab GTPase interactors in Arabidopsis
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 ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2023-09-21 | PXD044263 | Pride
Arabidopsis Rab gtpase 
ProteomicsDevelopment of a multiplex targeted mass spectrometry assay to quantify levels of LRRK2 phosphorylated Rab substrates and Ser910 and Ser935 biomarker sites
Mutations that increase the protein kinase activity of LRRK2 are one of the most common causes of familial Parkinson's disease. LRRK2 phosphorylates a subset of Rab GTPases within their Switch-II motif, impacting interaction with effectors. We describe and validate a new, multiplex targeted mass spe...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-03-17 | PXD022662 | Pride
Rab-gtpases Parkinson's disease Lrrk2 Prm Lc-ms/ms 
ProteomicsDetection of structure-specific interactions of Rab GTPases
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 i...
ORGANISM(S): Homo sapiens (Human) 
2024-02-10 | PXD048849 | Pride
Lc-msms Interactome Mass spectrometry Limited proteolysis Structural proteomics Protein-protein interactions Proteomics Rab gtpases Structure-specific interactions 
UnknownRab proteins and Rab-associated proteins: major actors in the mechanism of protein-trafficking disorders.
Not available
S-EPMC2413085 | biostudies-literature
TranscriptomicsTranscription profiling of peripheral blood or primary finroblast cultures from choroideremia patients to determine if loss-of-function mutations in REP-1 affect intracellular vesicle transport in fibroblasts and monocytes of CHM patients
Choroideremia (CHM) is a progressive X-linked retinopathy caused by mutations in the CHM gene, which encodes Rab escort protein-1 (REP-1), an escort protein involved in the prenylation of Rabs. Under-prenylation of certain Rabs, as a result of loss of function mutations in REP-1, could affect vesicu...
ORGANISM(S): Homo sapiens 
2010-02-21 | E-GEOD-17549 | biostudies-arrayexpress
ProteomicsUsing HDX-MS to study Rab and Ral covalently bound to MRTX1257
Here we use HDX to study covalently modified Rab1a and RalA in both their apo states and bound to MRTX1257 to see how this compound affects the overall secondary structure of the proteins.
ORGANISM(S): Homo sapiens (Human) 
2025-03-10 | PXD041440 | Pride
Rab Hdx-ms Ral Hdx Gtpase 
ProteomicsHDX-MS of TRAPPII reveals a conserved Rab binding interface
We used hydrogen deuterium exchange mass spectrometry (HDX-MS) to define the interface of TRAPPII with three Rab GTPases (Rab1, Rab11, Rab43). These experiments were performed in the presence of EDTA to generate a nucleotide free stabilised Rab-GEF complex. Significant decreases in deuterium incorpo...
ORGANISM(S): Homo sapiens (Human) 
2020-12-11 | PXD020890 | Pride
Hdx-ms Trappii Gef Rab 
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