The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity.

doi:10.1083/jcb.202010065

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Article

The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity.

The Journal of cell biology - 4 Apr 2022

Stormo Adrienne E D, Shavarebi Farbod, FitzGibbon Molly, Earley Elizabeth M, Ahrendt Hannah, Lum Lotus S, Verschueren Erik, Swaney Danielle L, Skibinski Gaia, Ravisankar Abinaya, van Haren Jeffrey, Davis Emily J, Johnson Jeffrey R, Von Dollen John, Balen Carson, Porath Jacob, Crosio Claudia, Mirescu Christian, Iaccarino Ciro, Dauer William T, Nichols R Jeremy, Wittmann Torsten, Cox Timothy C, Finkbeiner Steve, Krogan Nevan J, Oakes Scott A, Hiniker Annie

Abstract excerpt

Missense mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of familial Parkinson's disease (PD); however, pathways regulating LRRK2 subcellular localization, function, and turnover are not fully defined. We performed quantitative mass spectrometry-based interactome studies to identify 48 novel LRRK2 interactors, including the microtubule-associated E3 ubiquitin ligase TRIM1 (tripartite...

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Identifiers

PMID: 35266954
DOI: 10.1083/jcb.202010065
PMCID: PMC8919618

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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.

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