Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dissecting the effects of GTPase and kinase domain mutations on LRRK2 endosomal localization and activity.

Cell reports - 30 May 2023

Rinaldi Capria, Waters Christopher S, Li Zizheng, Kumbier Karl, Rao Lee, Nichols R Jeremy, Jacobson Matthew P, Wu Lani F, Altschuler Steven J

Abstract excerpt

Parkinson's disease-causing leucine-rich repeat kinase 2 (LRRK2) mutations lead to varying degrees of Rab GTPase hyperphosphorylation. Puzzlingly, LRRK2 GTPase-inactivating mutations-which do not affect intrinsic kinase activity-lead to higher levels of cellular Rab phosphorylation than kinase-activating mutations. Here, we investigate whether mutation-dependent differences in LRRK2 cellular localization could...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphorylation

Share to Protein Serine-Threonine Kinases

Share to rab GTP-Binding Proteins

Source

Identifiers

PMID: 37141099
DOI: 10.1016/j.celrep.2023.112447

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dissecting the effects of GTPase and kinase domain mutations on LRRK2 endosomal localization and activity.PMID 37141099Read ↗

Dissecting the effects of GTPase and kinase domain mutations on LRRK2 endosomal localization and activitySemantic proximity Read ↗

The G2019S variant of leucine-rich repeat kinase 2 (LRRK2) alters endolysosomal trafficking by impairing the function of the GTPase RAB8ASemantic proximity Read ↗

LRRK2: from kinase to GTPase to microtubules and back.Semantic proximity Read ↗

LRRK2 phosphorylates membrane-bound Rabs and is activated by GTP-bound Rab7L1 to promote recruitment to the trans-Golgi network.Semantic proximity Read ↗

The Role of LRRK2 in Intracellular Organelle Dynamics.Semantic proximity Read ↗

LRRK2 kinase dependent and independent function on endolysosomal repair promotes macrophage cell deathSemantic proximity Read ↗

Cellular functions of LRRK2 implicate vesicular trafficking pathways in Parkinson's disease.Semantic proximity Read ↗

Dysregulated phosphorylation of Rab GTPases by LRRK2 induces neurodegeneration.Semantic proximity Read ↗

Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations.Semantic proximity Read ↗

Cellular effects mediated by pathogenic LRRK2: homing in on Rab-mediated processes.Semantic proximity Read ↗

Distinct roles for RAB10 and RAB29 in pathogenic LRRK2-mediated endolysosomal trafficking alterationsSemantic proximity Read ↗

Elucidating the molecular interplay between LRRK2 and Rab GTPasesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.