Evidence map›Paper›PMID 33044192›Full record

ReviewJournal of Parkinson's disease2020

LRRK2 and the Endolysosomal System in Parkinson's Disease.

Madalynn L Erb, Darren J Moore

Open access · greenAbstract readReview
In one paragraph

Review in Journal of Parkinson's disease, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.1field-weighted citation impact, top 3% of its field
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

66 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Lysosomal homeostasis at the crossroads of neurodegeneration.The Journal of clinical investigation · 2026
    Review
  7. Review
  8. LRRK2 as a Potential Disease-Modifying Target in Sporadic Parkinson's Disease.Movement disorders : official journal of the Movement Disorder Society · 2026
    Review
  9. Integrated Biofluid Proteomics Identified Dynamic Functional Biomarkers ofmedRxiv : the preprint server for health sciences · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Neuroprotection in Parkinson Disease.Neurology and therapy · 2025
    Review
  16. Autophagic stress activates distinct compensatory secretory pathways in neurons.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Review

6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Madalynn L ErbCenter for Neurodegenerative Science, Van Andel Institute, Grand Rapids, MI, USA.
Darren J MooreCenter for Neurodegenerative Science, Van Andel Institute, Grand Rapids, MI, USA.
Van Andel Institute · US

Funding

Exploring mechanisms of Parkinson's disease-linked D620N VPS35 in rat modelsR01NS117137 · NINDS · VAN ANDEL RESEARCH INSTITUTE · PI MOORE, DARREN JOHN · 2020 to 2024
$2.2M
Novel Mechanisms of LRRK2-Dependent Neurodegeneration in Parkinson's DiseaseR01NS091719 · NINDS · VAN ANDEL RESEARCH INSTITUTE · PI MOORE, DARREN JOHN · 2015 to 2019
$2.1M
Mechanisms of VPS35-Dependent Neurodegeneration in Parkinson's DiseaseR01NS105432 · NINDS · VAN ANDEL RESEARCH INSTITUTE · PI MOORE, DARREN JOHN · 2017 to 2021
$2.1M
NINDS NIH HHS R01 NS091719NINDS NIH HHS R01 NS105432NINDS NIH HHS R01 NS117137
6 · The paper itself

Abstract

Mutations in leucine-rich repeat kinase 2 (LRRK2) cause autosomal dominant familial Parkinson's disease (PD), with pathogenic mutations enhancing LRRK2 kinase activity. There is a growing body of evidence indicating that LRRK2 contributes to neuronal damage and pathology both in familial and sporadic PD, making it of particular interest for understanding the molecular pathways that underlie PD. Although LRRK2 has been extensively studied to date, our understanding of the seemingly diverse functions of LRRK2 throughout the cell remains incomplete. In this review, we discuss the functions of LRRK2 within the endolysosomal pathway. Endocytosis, vesicle trafficking pathways, and lysosomal degradation are commonly disrupted in many neurodegenerative diseases, including PD. Additionally, many PD-linked gene products function in these intersecting pathways, suggesting an important role for the endolysosomal system in maintaining protein homeostasis and neuronal health in PD. LRRK2 activity can regulate synaptic vesicle endocytosis, lysosomal function, Golgi network maintenance and sorting, vesicular trafficking and autophagy, with alterations in LRRK2 kinase activity serving to disrupt or regulate these pathways depending on the distinct cell type or model system. LRRK2 is critically regulated by at least two proteins in the endolysosomal pathway, Rab29 and VPS35, which may serve as master regulators of LRRK2 kinase activity. Investigating the function and regulation of LRRK2 in the endolysosomal pathway in diverse PD models, especially in vivo models, will provide critical insight into the cellular and molecular pathophysiological mechanisms driving PD and whether LRRK2 represents a viable drug target for disease-modification in familial and sporadic PD.

Indexed as

Parkinson DiseaseAnimalsEndocytosisEndosomesHumansLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LysosomesSignal Transductiontrans-Golgi NetworkLeucine-Rich Repeat Serine-Threonine Protein Kinase-2LRRK2 protein, humanendocytosisLeucine-rich repeat kinase 2lysosomesParkinson’s diseasetrans-Golgi networkvesicular trafficking

Identifiers

PMID33044192
PMCPMC7677880
OpenAlexW3092006859

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.