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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 
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 
ProteomicsStructural basis for the specificity of PPM1H phosphatase for Rab GTPases
LRRK2 serine/threonine kinase is associated with inherited Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases within their switch 2 motif to control their interactions with effectors. Recent work has shown that the metal-dependent protein phosphatase PPM1H counteracts LRRK2 by dephosp...
ORGANISM(S): Homo sapiens (Human) 
2021-08-11 | PXD026367 | Pride
Rab8a Ppm1h Dsbu crosslinking 
ProteomicsPhosphoproteomics reveals that Parkinson’s disease kinase LRRK2 regulates a subset of Rab GTPases
Mutations in Park8, encoding for the multidomain Leucine-rich repeat kinase 2 (LRRK2) protein, comprise the predominant genetic cause of Parkinson’s disease (PD). G2019S, the most common amino acid substitution activates the kinase two to three-fold. This has motivated the development of LRRK2 kinas...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2016-02-04 | PXD003071 | Pride
Lrrk2 Substrates Phosphoproteomics Rab gtpases 
UnknownRab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.
Not available
S-EPMC5902227 | biostudies-literature
UnknownRab GTPases and tethering in the yeast endocytic pathway.
Not available
S-EPMC3136951 | biostudies-literature
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 
UnknownAre There Rab GTPases in Archaea?
Not available
S-EPMC4915359 | biostudies-literature
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