ArticleThe Biochemical journal2010
14-3-3 proteins are promising LRRK2 interactors.
Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Leucine-rich repeat kinase 2 at a glance.Journal of cell science · 2023Article
- The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity.The Journal of cell biology · 2022Article
- The Parkinson's disease-linked Leucine-rich repeat kinase 2 (LRRK2) is required for insulin-stimulated translocation of GLUT4.Scientific reports · 2019Article
- The unlikely partnership between LRRK2 and α-synuclein in Parkinson's disease.The European journal of neuroscience · 2019Review
- Roco Proteins: GTPases with a Baroque Structure and Mechanism.International journal of molecular sciences · 2019Review
- LRRK2, a puzzling protein: insights into Parkinson's disease pathogenesis.Experimental neurology · 2014Review
- Pathway for Parkinson disease.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Synaptic function is modulated by LRRK2 and glutamate release is increased in cortical neurons of G2019S LRRK2 knock-in mice.Frontiers in cellular neuroscience · 2014Article
- A53T-alpha-synuclein-overexpression in the mouse nigrostriatal pathway leads to early increase of 14-3-3 epsilon and late increase of GFAP.Journal of neural transmission (Vienna, Austria : 1996) · 2012Article
- 14-3-3 proteins in neurological disorders.International journal of biochemistry and molecular biology · 2012Article
- 14-3-3 proteins as potential therapeutic targets.Seminars in cell & developmental biology · 2011Review
- Models for LRRK2-Linked Parkinsonism.Parkinson's disease · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in LRRK2 (leucine-rich repeat kinase 2) are the most common cause of familial PD (Parkinson's disease). Mutations that cause PD are found in either the GTPase or kinase domains of LRRK2 or an intervening sequence called the COR [C-terminus of ROC (Ras of complex proteins)] domain. As well as the two catalytic domains, LRRK2 possesses several protein-protein interaction domains, but their function and the proteins with which they interact are poorly understood. In this issue of the Biochemical Journal, Nichols et al. study the interaction of the N-terminal region of LRRK2 with 14-3-3 proteins, regulatory proteins that often bind to phosphorylated regions of components of cell signalling pathways. Using a combination of techniques, Nichols et al. have identified two residues (Ser910 and Ser935) that are critically responsible for 14-3-3 binding. The interaction of LRRK2 with 14-3-3 proteins can prevent dephosphorylation of Ser910/Ser935 and stabilize LRRK2 structure, perhaps by influencing the dimerization of LRRK2. The ability to interact with 14-3-3 correlates with the pattern of intracellular LRRK2 distribution. Collectively, these new results identify a potentially important regulatory mechanism of this complex protein and might provide ways to think about therapeutic opportunities for PD.
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Registered trials
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.