Nature Communications (Jun 2016)
Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1
- Frederick C. Nucifora,
- Leslie G. Nucifora,
- Chee-Hoe Ng,
- Nicolas Arbez,
- Yajuan Guo,
- Elaine Roby,
- Vered Shani,
- Simone Engelender,
- Dong Wei,
- Xiao-Fang Wang,
- Tianxia Li,
- Darren J. Moore,
- Olga Pletnikova,
- Juan C. Troncoso,
- Akira Sawa,
- Ted M. Dawson,
- Wanli Smith,
- Kah-Leong Lim,
- Christopher A. Ross
Affiliations
- Frederick C. Nucifora
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Leslie G. Nucifora
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Chee-Hoe Ng
- Danone Nutricia Research
- Nicolas Arbez
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Yajuan Guo
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Elaine Roby
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Vered Shani
- Department of Molecular Pharmacology, Rappaport Institute of Medical Research, Technion-Israel Institute of Technology
- Simone Engelender
- Department of Molecular Pharmacology, Rappaport Institute of Medical Research, Technion-Israel Institute of Technology
- Dong Wei
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Xiao-Fang Wang
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Tianxia Li
- Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy
- Darren J. Moore
- Center for Neurodegenerative Science, Van Andel Research Institute
- Olga Pletnikova
- Division of Neuropathology, Department of Pathology, Johns Hopkins University School of Medicine
- Juan C. Troncoso
- Division of Neuropathology, Department of Pathology, Johns Hopkins University School of Medicine
- Akira Sawa
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- Ted M. Dawson
- Department of Neurology, Johns Hopkins University School of Medicine
- Wanli Smith
- Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy
- Kah-Leong Lim
- Neuroscience and Behavioral Disorders Program, Duke-National University of Singapore Graduate Medical School
- Christopher A. Ross
- Department of Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine
- DOI
- https://doi.org/10.1038/ncomms11792
- Journal volume & issue
-
Vol. 7,
no. 1
pp. 1 – 11
Abstract
Mutations in LRRK2 are linked to Parkinson’s Disease. Here, the authors identify WSB1 as a LRRK2 interacting protein and find that it promotes LRRK2 aggregation in primary neurons and drosophila models via ubiquitin K27 and K29 linkages.
