Closing the structure-to-function gap for LRRK2

Valerie Tokars; Chuyu Chen; Loukia Parisiadou

doi:10.1016/j.tibs.2021.10.003

Closing the structure-to-function gap for LRRK2

Trends Biochem Sci. 2022 Mar;47(3):187-188. doi: 10.1016/j.tibs.2021.10.003. Epub 2021 Oct 28.

Authors

Valerie Tokars¹, Chuyu Chen¹, Loukia Parisiadou²

Affiliations

¹ Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA.
² Department of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, IL, USA. Electronic address: loukia.parisiadou@northwestern.edu.

PMID: 34756665
DOI: 10.1016/j.tibs.2021.10.003

Abstract

Variations in the LRRK2 gene represent one of the strongest genetic factors for Parkinson's disease (PD). It has become clear that structural knowledge of the encoded large multidomain LRRK2 protein will cast light on its biological function. The new study from Myasnikov, Zhu, et al. provides a high-resolution structure of the full-length LRRK2.

Keywords: Parkinson's disease; cryo-EM; full-length leucine-rich repeat kinase 2 (LRRK2); high-resolution structure.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Humans
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 / chemistry
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 / genetics
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 / metabolism
Mutation
Parkinson Disease* / genetics
Parkinson Disease* / metabolism

Substances

LRRK2 protein, human
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

Grants and funding

R01 NS097901/NS/NINDS NIH HHS/United States