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Pathogenic LRRK2 regulates ciliation probability upstream of tau tubulin kinase 2 via Rab10 and RILPL1 proteins

descriptionPublicationkeyboard_double_arrow_right Article , Other literature type 02 Mar 2021 English Publisher:Proceedings of the National Academy of SciencesJournal:Proceedings of the National Academy of Sciences, volume 118 (issn: 0027-8424, eissn: 1091-6490,

Authors: Yuriko Sobu; Paulina S. Wawro; Herschel S. Dhekne; Wondwossen M. Yeshaw; Suzanne R. Pfeffer;

doi: 10.1073/pnas.2005894118

pmid: 33653948

pmc: PMC7958464

Pathogenic LRRK2 regulates ciliation probability upstream of tau tubulin kinase 2 via Rab10 and RILPL1 proteins

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Abstract

Significance Mutations that activate LRRK2 protein kinase cause Parkinson's disease. LRRK2 phosphorylates a subset of Rab GTPases, in particular Rab8 and Rab10. We show here details related to the mechanism by which Rab10 phosphorylation blocks initiation of cilia formation, fundamental information related to how pathogenic LRRK2 interferes with normal cell physiology.

Related Organizations

Stanford University School of Medicine
United States
Stanford University
United States
Department of Biochemistry Stanford University School of Medicine
United States

Keywords

Mutation, Missense, Mice, Transgenic, Parkinson Disease, Biological Sciences, Protein Serine-Threonine Kinases, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Mice, Amino Acid Substitution, rab GTP-Binding Proteins, Animals, Cilia, Adaptor Proteins, Signal Transducing

9 Research products, page 1 of 1

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	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	62
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	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Top 10%
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 1%