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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 
UnknownParkinson's VPS35[D620N] mutation induces LRRK2-mediated lysosomal association of RILPL1 and TMEM55B.
Not available
S-EPMC10848721 | biostudies-literature
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 
UnknownThe Rilp-like proteins Rilpl1 and Rilpl2 regulate ciliary membrane content.
Not available
S-EPMC3571868 | biostudies-literature
UnknownPathogenic LRRK2 regulates centrosome cohesion via Rab10/RILPL1-mediated CDK5RAP2 displacement.
Not available
S-EPMC9198432 | biostudies-literature
UnknownA large pedigree study confirmed the CGG repeat expansion of RILPL1 Is associated with oculopharyngodistal myopathy.
Not available
S-EPMC10590002 | biostudies-literature
ProteomicsParkinson’s VPS35[D620N] retromer lysosomal dysfunction induces LRRK2 mediated lysosomal association of RILPL1 and TMEM55B
The D620N VPS35 mutation disrupts retrograde endosome to Golgi retromer Trafficking. Thus causes lysosome dysfunction, enhances LRRK2 kinase activity and leads to Parkinson’s disease. We employed a LysoTag immunoprecipitation approach to assess how this impacts lysosomes using quantitative proteomic...
ORGANISM(S): Mus musculus (Mouse) 
2023-11-28 | PXD042502 | Pride
Parinson's disease  lysosomal proteins  lrrk2  rilpl1  tmem55b 
UnknownStructural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved TBM motif.
Not available
S-EPMC12393467 | biostudies-literature
UnknownJIP4 and RILPL1 utilize opposing motor force to dynamically regulate lysosomal tubulation.
Not available
S-EPMC12459091 | biostudies-literature
UnknownPathogenic LRRK2 regulates ciliation probability upstream of tau tubulin kinase 2 via Rab10 and RILPL1 proteins.
Not available
S-EPMC7958464 | biostudies-literature
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