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

Regulation of LRRK2 mRNA stability by ATIC and its substrate AICAR through ARE-mediated mRNA decay in Parkinson's disease.

The EMBO journal - 1 Aug 2023

Liu Qinfang, Zhu Dong, Li Naren, Chen Shifan, Hu Liang, Yu Jianzhong, Xiong Yulan

Abstract excerpt

Mutations in LRRK2 are the most common genetic causes of Parkinson's disease (PD). While the enzymatic activity of LRRK2 has been linked to PD, previous work has also provided support for an important role of elevated LRRK2 protein levels, independent of enzymatic activity, in PD pathogenesis. However, the mechanisms underlying the regulation of LRRK2 protein levels remain unclear. Here, we identify a role for...

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 Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Parkinson Disease

Share to Protein Serine-Threonine Kinases

Share to RNA, Messenger

Share to RNA Stability

Source

Open in PubMed Open full text

Identifiers

PMID: 37366237
DOI: 10.15252/embj.2022113410
PMCID: PMC10390876

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Regulation of LRRK2 mRNA stability by ATIC and its substrate AICAR through ARE-mediated mRNA decay in Parkinson's disease.PMID 37366237Read ↗

Targeting LRRK2 mRNA stability in Parkinson's disease.Semantic proximity Read ↗

Alternative cleavage and polyadenylation of genes associated with protein turnover and mitochondrial function are deregulated in Parkinson’s, Alzheimer’s and ALS diseaseSemantic proximity Read ↗

LRRK2 PROTAC Degraders as a Potential Novel Targeting Strategy for Parkinson's Disease?Semantic proximity Read ↗

A high-throughput screen identifies the long non-coding RNA DRAIC as a regulator of autophagySemantic proximity Read ↗

ADAR2 mislocalization and widespread RNA editing aberrations in C9orf72-mediated ALS/FTDSemantic proximity Read ↗

LRRK2-mediated phosphorylation of HDAC6 regulates HDAC6-cytoplasmic dynein interaction and aggresome formationSemantic proximity Read ↗

Gene and MicroRNA transcriptome analysis of Parkinson's related LRRK2 mouse models.Semantic proximity Read ↗

Direct binding of Ataxin-2 to distinct elements in 3' UTRs promotes mRNA stability and protein expression.Semantic proximity Read ↗

SETX (senataxin), the helicase mutated in AOA2 and ALS4, functions in autophagy regulationSemantic proximity Read ↗

Profound downregulation of the RNA editing enzyme ADAR2 in ALS spinal motor neuronsSemantic proximity Read ↗

Lafora disease E3 ubiquitin ligase malin is recruited to the processing bodies and regulates the microRNA-mediated gene silencing process via the decapping enzyme Dcp1aSemantic proximity Read ↗

DPP8/9 processing of human AK2 unmasks an IAP binding motifSemantic proximity Read ↗

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