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

The Journal of Cell Biology(2022)10.1083/jcb.202010065Source: DataRank Database

The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity is a research paper published in The Journal of Cell Biology (2022). On theSindex it has a DataRank of 0. It has been cited 18 times.

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Open Access18 citations

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Enrichment:Funding (27 grants)OA: hybridTopics (43)IDs (PubMed, PMC)Annotations (1)

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Authors (27)

Farbod Shavarebi ORCID,Molly FitzGibbon,Elizabeth M. Earley,Hannah Ahrendt ORCID,Lotus Lum ORCID

Live enrichment

PubMed:35266954 PMC:PMC8919618

UCSF Parnassus Flow Cytometry Core

Grant: SCR_018206

DRC Center

Grant: NIG P30 DK063720

DRC Center

Grant: RF1 AG058476

DRC Center

Grant: P01 AG054407

DRC Center

Grant: R01 NS124848

Fondazione Banco di Sardegna

Grant: 2014.0489

Fondo di Ateneo per la Ricerca

Grant: S10 RR026758

National Institutes of Health

Grant: R01EY027810

National Institutes of Health

Grant: R01CA219815

National Institutes of Health

Grant: K08NS090633

DoD

Grant: W81XWH-18-1-0376

NINDS NIH HHS

Grant: R01 NS107480

NINDS NIH HHS

Grant: RF1 NS124848

NIDDK NIH HHS

Grant: P30 DK063720

National Institutes of Health

Grant: 7K08NS090633-06

Chemical-Genetic Approaches to Define Lrrk2 Kinase Function in Parkinson Disease

National Institutes of Health

Grant: 4R01NS124848-02

Dissecting the Etiology of The Lewy Body Dementias

National Institutes of Health

Grant: 5R01EY027810-02

Role of the Unfolded Protein Response in Photoreceptor Degeneration

National Institutes of Health

Grant: 1R01CA219815-01A1

Targeting the Unfolded Protein Response in PanNETs

National Institutes of Health

Grant: 5P30DK063720-03

ISLET PRODUCTION FACILITY CORE

National Institutes of Health

Grant: 3RF1AG058476-01S4

Dysfunction of the Autophagy-Lysosomal Pathway as a Common Mechanism of Neurodegeneration

National Institutes of Health

Grant: 1S10RR026758-01

Spinning disk confocal / FRAP microscope for quantitative live cell imaging

National Institutes of Health

Grant: 5P01AG054407-04

Proteostasis in Aging and Neurodegenerative Disease

Laurel Endowment

Stowers Family Endowed Chair for Dental & Mineralized Tissue Research

American Federation for Aging Research

Michael J Fox Foundation

Taube Koret Center

hybridLicense: CC BY

publisherhttps://rupress.org/jcb/article-pdf/doi/10.1083/jcb.202010065/1616236/jcb_202010065.pdf

Unpaywallhttps://rupress.org/jcb/article-pdf/221/4/e202010065/1429684/jcb_202010065.pdf

Europe_PMChttps://europepmc.org/articles/PMC8919618

Europe_PMChttps://europepmc.org/articles/PMC8919618?pdf=render

https://doi.org/10.1083/jcb.202010065

Fields of Study

0301 basic medicine03 medical and health sciences

MeSH Terms

CytoskeletonMicrotubulesHumansParkinson Diseaserab GTP-Binding ProteinsUbiquitin-Protein LigasesMicrotubule-Associated ProteinsTranscription FactorsPhosphorylationMutationUbiquitinationTripartite Motif ProteinsLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Protein Serine-Threonine Kinases

Keywords

Ubiquitin-Protein Ligases610NeurodegenerativeProtein Serine-Threonine KinasesLeucine-Rich Repeat Serine-Threonine Protein Kinase-2Medical and Health SciencesMicrotubulesArticleTripartite Motif Proteins2.1 Biological and endogenous factorsHumansAetiologyPhosphorylationCytoskeletonParkinson's DiseaseNeurosciencesUbiquitinationParkinson DiseaseBiological SciencesBrain Disordersrab GTP-Binding ProteinsNeurologicalMutationLrrk2, Parkinson’s disease, microtubule-associated E3 ubiquitin ligase TRIM1Microtubule-Associated ProteinsDevelopmental BiologyTranscription Factors