Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2.

Gaussian accelerated molecular dynamics Parkinson’s disease hydrogen-deuterium exchange mass spectrometry (HDX-MS) kinase regulation leucine-rich repeat kinase 2 (LRRK2)

Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
08 06 2021
Historique:
entrez: 5 6 2021
pubmed: 6 6 2021
medline: 1 12 2021
Statut: ppublish

Résumé

To explore how pathogenic mutations of the multidomain leucine-rich repeat kinase 2 (LRRK2) hijack its finely tuned activation process and drive Parkinson's disease (PD), we used a multitiered approach. Most mutations mimic Rab-mediated activation by "unleashing" kinase activity, and many, like the kinase inhibitor MLi-2, trap LRRK2 onto microtubules. Here we mimic activation by simply deleting the inhibitory N-terminal domains and then characterize conformational changes induced by MLi-2 and PD mutations. After confirming that LRRK2

Identifiants

pubmed: 34088839
pii: 2100844118
doi: 10.1073/pnas.2100844118
pmc: PMC8201809
pii:
doi:

Substances chimiques

LRRK2 protein, human EC 2.7.11.1
Leucine-Rich Repeat Serine-Threonine Protein Kinase-2 EC 2.7.11.1

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIGMS NIH HHS
ID : P41 GM103412
Pays : United States
Organisme : NIGMS NIH HHS
ID : R24 GM137200
Pays : United States
Organisme : NIH HHS
ID : S10 OD016234
Pays : United States
Organisme : NINDS NIH HHS
ID : U24 NS120055
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009523
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM086197
Pays : United States

Informations de copyright

Copyright © 2021 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Sven H Schmidt (SH)

Department of Biochemistry, University of Kassel, 34132 Kassel, Germany.

Jui-Hung Weng (JH)

Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093.

Phillip C Aoto (PC)

Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093.
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093.

Daniela Boassa (D)

National Center for Microscopy and Imaging Research, University of California, San Diego, La Jolla, CA 92093.
Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093.

Sebastian Mathea (S)

Institute for Pharmaceutical Chemistry, Johann Wolfgang Goethe-University, D-60438 Frankfurt am Main, Germany.

Steve Silletti (S)

Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093.

Junru Hu (J)

National Center for Microscopy and Imaging Research, University of California, San Diego, La Jolla, CA 92093.
Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093.

Maximilian Wallbott (M)

Department of Biochemistry, University of Kassel, 34132 Kassel, Germany.

Elizabeth A Komives (EA)

Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093.

Stefan Knapp (S)

Institute for Pharmaceutical Chemistry, Johann Wolfgang Goethe-University, D-60438 Frankfurt am Main, Germany.
Structural Genomics Consortium, Buchmann Institute for Molecular Life Sciences, Johann Wolfgang Goethe-University, D-60438 Frankfurt am Main, Germany.

Friedrich W Herberg (FW)

Department of Biochemistry, University of Kassel, 34132 Kassel, Germany; herberg@uni-kassel.de staylor@ucsd.edu.

Susan S Taylor (SS)

Department of Pharmacology, University of California, San Diego, La Jolla, CA 92093; herberg@uni-kassel.de staylor@ucsd.edu.
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093.

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