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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 
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 
UnknownAre There Rab GTPases in Archaea?
Not available
S-EPMC4915359 | biostudies-literature
ProteomicsTargeting Ras-, Rho-, and Rab-Family GTPases via a Conserved Cryptic Pocket
The family of Ras-like GTPases consists of over 150 different members, regulated by an even larger number of guanine exchange factors (GEFs) and GTPase-activating proteins (GAPs) which comprise cellular switch networks that govern cell motility, growth, polarity, protein trafficking, and gene expres...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD054414 | Pride
Gtpase 
UnknownDysregulated phosphorylation of Rab GTPases by LRRK2 induces neurodegeneration.
Not available
S-EPMC5811984 | biostudies-literature
ProteomicsArginine GlcNAcylation of Rab small GTPases by the pathogen Salmonella Typhimurium
We determined the GlcNAcyaltion of Rab1 by a Salmonella T3SS effector SseK3. IP experiments were performed from HEK293 cells and MS files were acquired on Q Exactive mass spectrometer. We analysed the differences of protein abundance, comparing the normalized intensity on distinct proteins from diff...
ORGANISM(S): Homo Sapiens Escherichia Coli Mus Musculus 
2020-06-05 | PXD019062 |
UnknownRegulation of Golgi Cisternal Progression by Ypt/Rab GTPases.
Not available
S-EPMC4768313 | biostudies-literature
UnknownIntegrin-mediated function of Rab GTPases in cancer progression.
Not available
S-EPMC3003658 | biostudies-literature
UnknownDual arginine recognition of LRRK2 phosphorylated Rab GTPases.
Not available
S-EPMC8204342 | biostudies-literature
UnknownRab GTPases in Osteoclastic Endomembrane Systems.
Not available
S-EPMC6114073 | biostudies-literature
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