Evidence map›Paper›PMID 40909700›Full record

ArticlebioRxiv : the preprint server for biology2025

Leucine-rich repeat kinase 2 impairs the release sites of Parkinson's disease vulnerable dopamine axons.

Chuyu Chen, Qianzi He, Giulia Tombesi, Eve Napier, Matthew Jaconelli, Oscar Andrés Moreno-Ramos, Hannah Serio, Yahaira Naaldijk, Vanessa Promes, Amanda Schneeweis and 11 more

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

21 authors.

Chuyu ChenDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0000-0001-5666-5173
Qianzi HeDepartment of Neurobiology, Northwestern University, Evanston, IL, USA.ORCID 0000-0002-4607-166X
Giulia TombesiDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0000-0003-0683-8050
Eve NapierSchool of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.ORCID 0000-0002-2667-2652
Matthew JaconelliMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, Scotland, United Kingdom.ORCID 0009-0003-1536-435X
Oscar Andrés Moreno-RamosDepartment of Neurology, Northwestern University, Chicago, IL, USA.ORCID 0000-0002-1378-2545
Hannah SerioDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0000-0002-9845-3205
Yahaira NaaldijkDepartment of Anesthesiology, Rutgers, New Jersey Medical School, NJ, USA.ORCID 0000-0003-2701-3963
Vanessa PromesDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0000-0002-9078-6232
Amanda SchneeweisDepartment of Neurology, Northwestern University, Chicago, IL, USA.ORCID 0000-0003-4141-6064
Kaitlyn QuinnDepartment of Neurobiology, Northwestern University, Evanston, IL, USA.ORCID 0009-0000-7931-742X
Christopher NasiosDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0009-0005-2246-787X
Elisa GreggioDepartment of Biology, University of Padova, Italy.ORCID 0000-0002-8172-3598
Yevgenia KozorovitskiyDepartment of Neurobiology, Northwestern University, Evanston, IL, USA.ORCID 0000-0002-3710-1484
Daniel ArangoDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0000-0001-9523-830X
Amir R KhanSchool of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.ORCID 0000-0003-1176-6952
Dario R AlessiMedical Research Council Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, Scotland, United Kingdom.ORCID 0000-0002-2140-9185
Daniel A DombeckDepartment of Neurobiology, Northwestern University, Evanston, IL, USA.ORCID 0000-0003-2576-5918
Sabine HilfikerDepartment of Anesthesiology, Rutgers, New Jersey Medical School, NJ, USA.ORCID 0000-0002-5167-7682
Rajeshwar AwatramaniDepartment of Neurology, Northwestern University, Chicago, IL, USA.ORCID 0000-0002-0713-2140
Loukia ParisiadouDepartment of Pharmacology, Northwestern University, Chicago, IL, USA.ORCID 0000-0002-2569-4200

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Devalingam Mahalingam · 1993 to 2026
$153.9M
Developmental underpinnings of substantia nigra vulnerabilityR01NS119690 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI AWATRAMANI, RAJESHWAR B · 2021 to 2025
$2.4M
Nikon CSU W1 SoRa for the Center for Advanced Microscopy and Nikon Imaging Center at Northwestern UniversityS10OD032270 · OD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ARVANITIS, CONSTADINA · 2023 to 2023
$600k
Nikon Super-Resolution Structured Illumination Microscope (SIM)S10OD016342 · OD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI CHEW, TENG-LEONG · 2013 to 2013
$600k
NCI NIH HHS P30 CA060553NIH HHS S10 OD016342NIH HHS S10 OD032270NINDS NIH HHS R01 NS119690
6 · The paper itself

Abstract

The end-stage pathology of Parkinson's disease (PD) involves the loss of dopamine-producing neurons in the substantia nigra pars compacta (SNc). However, synaptic deregulation of these neurons begins much earlier. Understanding the mechanisms behind synaptic deficits is crucial for early therapeutic intervention, yet these remain largely unknown. In the SNc, different dopamine neuron subtypes show varying susceptibility patterns to PD, complicating our understanding. This study uses intersectional genetic mouse models to uncover synaptic perturbations in vulnerable dopamine neurons, focusing on the LRRK2 kinase, a protein closely linked to PD. Through a combination of immunofluorescence and advanced proximity labeling methods, we found higher LRRK2 expression in the most vulnerable dopamine neuron subclusters. High-resolution imaging revealed that pathogenic LRRK2 disrupts release sites in vulnerable dopamine axons, leading to decreased in vivo evoked striatal dopamine release in mice with LRRK2 mutations. Proteomic and biochemical analyses indicate that mutant LRRK2 increases the phosphorylation of RAB3 proteins, reducing their interactions with RIM1/2 effector proteins and impacting their synaptic functions. Overall, this research highlights the cell-autonomous dysfunctions caused by mutant LRRK2 in the neurons that are primarily affected by the disease. It also provides a framework for therapeutic strategies for early nigrostriatal synaptic deficits in PD.

Identifiers

PMID40909700
PMCPMC12407872

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.