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ProteomicsGolgi-IP, a novel tool for multimodal analysis of Golgi molecular content
The Golgi plays an essential role in protein and lipid glycosylation. Golgi dysfunction is associated with a variety of diseases including cancer, neurodegeneration and cardiovascular disease. We developed a powerful immunoprecipitation technique to isolate the Golgi by tagging TMEM115. Golgi-immuno...
ORGANISM(S): Homo sapiens (Human) 
2023-04-24 | PXD038046 | Pride
Golgi-ip Proteomics Metabolomics Lipidomics Golgi apparatus 
ProteomicsCURTAIN – A Unique Web-based tool for exploration and sharing of MS-based proteomics data
To facilitate analysis and sharing of mass spectrometry (MS)-based proteomics data we created two tools called CURTAIN (https://curtain.proteo.info) and CURTAIN-PTM (https://curtainptm.proteo.info). They are designed to enable the non-MS expert to interactively pursue volcano plots, deconvolute prim...
ORGANISM(S): Homo sapiens (Human) 
2023-12-21 | PXD043806 | Pride
Bioinformatics Ptm Bromotag Proteomics 
ProteomicsPKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain
Leucine-rich-repeat-kinase 1 (LRRK1) and its homologue LRRK2 are multidomain kinases possessing an atypical ROC-CORA-CORB containing GTPase domain and phosphorylate distinct Rab proteins. LRRK1 loss of function mutations cause the bone disorder osteosclerotic metaphyseal dysplasia, whereas LRRK2 mis...
ORGANISM(S): Homo sapiens (Human) 
2022-09-02 | PXD034420 | Pride
Rab7a Lrrk1 Pkc Phosphorylation 
ProteomicsDiscovery of XL01126: A Potent, Fast, Cooperative, Selective, Oral bioavailable and Blood Brain Barrier Penetrant PROTAC Degrader of Leucine Rich Repeat Kinase 2 (LRRK2)
Leucine Rich Repeat Kinase 2 (LRRK2) is one of the most promising targets for Parkinson’s Disease. LRRK2 targeting strategies have primarily focused on Type 1 kinase inhibitors, which however have limitations as the inhibited protein can interfere with natural mechanisms and lead to undesirable side...
ORGANISM(S): Mus musculus (Mouse) 
2022-09-02 | PXD034055 | Pride
Parkinsosn's disease Tmt Lrrk2 Mass spectrometry Protac 
ProteomicsParkinson’s VPS35[D620N] mutation induces LRRK2 mediated lysosomal association of RILPL1 and TMEM55B
The Parkinson’s VPS35[D620N] mutation causes lysosome dysfunction enhancing LRRK2 kinase activity. We find the VPS35[D620N] mutation alters expression of ~350 lysosomal proteins and stimulates LRRK2 recruitment and phosphorylation of Rab proteins at the lysosome. This recruits the phosphoRab effecto...
ORGANISM(S): Homo sapiens (Human) 
2023-11-08 | PXD045671 | Pride
Parkinson's disease Lrrk2 Lysosome Proteomics 
ProteomicsTagless LysoIP method for molecular profiling of lysosomal content in clinical samples
Lysosomes are implicated in a wide spectrum of human diseases including monogenic lysosomal storage disorders (LSDs), age-associated neurodegeneration and cancer. Profiling lysosomal content using tag-based lysosomal immunopurification (LysoIP) in cell and animal models allowed major discoveries in ...
ORGANISM(S): Homo sapiens (Human) 
2025-01-31 | PXD052082 | Pride
Metabolomics Proteomics Dia Lysosomal storage disorder Lipidomics Lysosome Mass spectrometry 
ProteomicsStructural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved TBM motif
Inherited mutations in VPS35 and the kinase LRRK2 lead to hyperphosphorylation of Rab GTPases and promote the formation of phospho-Rab signalling complexes. A subset of RH2 domain-containing proteins from the RILP-homology family, including RILP, RILPL1, RILPL2, JIP3, and JIP4 are Rab effectors that...
ORGANISM(S): Homo sapiens (Human) 
2025-11-30 | PXD067414 | Pride
Lysosome Lrrk2 Tmem55b Parkinson's disease Structure 
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 
ProteomicsPPM1H phosphatase counteracts LRRK2 signaling by selectively dephosphorylating Rab proteins
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...
ORGANISM(S): Homo sapiens (Human) 
2019-11-06 | PXD014794 | Pride
Lrrk2 Phosphatase Parkinson's disease Rab10 
ProteomicsBiochemical characterization of protease activity of Nsp3 from SARS-CoV-2 and its inhibition by nanobodies
Of the 16 non-structural proteins (Nsps) encoded by SARS CoV-2, Nsp3 is the largest and plays important roles in the viral life cycle. Being a large, multidomain, transmembrane protein, Nsp3 has been the most challenging to characterize. Encoded within the multidomain Nsp3 is the papain-like proteas...
ORGANISM(S): Homo sapiens (Human) 
2021-09-15 | PXD022904 | Pride
Ubiqutylation Isg15 Sars cov-2 
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