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Apo C-terminal half of LRRK2 (I2020T) bound to microtubule

ABSTRACT:

SUBMITTER: Mariusz Matyszewski

PROVIDER: EMPIAR-10924 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural basis for Parkinson's disease-linked LRRK2's binding to microtubules.

Snead David M DM Matyszewski Mariusz M Dickey Andrea M AM Lin Yu Xuan YX Leschziner Andres E AE Reck-Peterson Samara L SL

Nature structural & molecular biology 20221212 12

Leucine-rich repeat kinase 2 (LRRK2) is one of the most commonly mutated genes in familial Parkinson's disease (PD). Under some circumstances, LRRK2 co-localizes with microtubules in cells, an association enhanced by PD mutations. We report a cryo-EM structure of the catalytic half of LRRK2, containing its kinase, in a closed conformation, and GTPase domains, bound to microtubules. We also report a structure of the catalytic half of LRRK1, which is closely related to LRRK2 but is not linked to P ...[more]

PMID: 36510024

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