Apoptotic mechanisms in mutant LRRK2-mediated cell death (original) (raw)

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1

Department of Physiological, Biochemical, and Cell Science

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University of Sassari

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Via Muroni 25, 07100 Sassari

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Italy

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Fondazione Santa Lucia IRCCS

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c/o CERC, Via del Fosso di Fiorano 64, 00143 Rome

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Italy

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Department of Physiological, Biochemical, and Cell Science

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University of Sassari

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Via Muroni 25, 07100 Sassari

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Italy

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Fondazione Santa Lucia IRCCS

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c/o CERC, Via del Fosso di Fiorano 64, 00143 Rome

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Italy

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Department of Neurological Science

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University of Naples ‘Federico II’

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Via Pansini 5, 80131 Naples

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Italy

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Istituto di Diagnostica e Cura ‘Hermitage’ Capodimonte

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Via Cupa Delle Tozzole, 2, 80143 Naples

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Italy

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Department of Physiological, Biochemical, and Cell Science

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University of Sassari

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Via Muroni 25, 07100 Sassari

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Italy

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Fondazione Santa Lucia IRCCS

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c/o CERC, Via del Fosso di Fiorano 64, 00143 Rome

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Italy

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Department of Biology

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University of Rome ‘Tor Vergata’

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Via della Ricerca Scientifica, 00133 Rome

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Italy

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Department of Neurological Science

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University of Naples ‘Federico II’

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Via Pansini 5, 80131 Naples

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Revision received:

29 January 2007

Received:

06 December 2007

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Ciro Iaccarino, Claudia Crosio, Carmine Vitale, Giovanna Sanna, Maria Teresa Carrì, Paolo Barone, Apoptotic mechanisms in mutant LRRK2-mediated cell death, Human Molecular Genetics, Volume 16, Issue 11, 1 June 2007, Pages 1319–1326, https://doi.org/10.1093/hmg/ddm080
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Abstract

Mutations in the gene coding for leucine-rich repeat kinase 2 (LRRK2) cause autosomal-dominant Parkinson's disease. The pathological mutations have been associated with an increase of LRRK2 kinase activity, although its physiological substrates have not been identified yet. The data we report here demonstrate that disease-associated mutant LRRK2 cell toxicity is due to mitochondria-dependent apoptosis. Transient transfection of mutant LRRK2 leads to neuronal death with clear apoptotic signs. Soluble caspase inhibitors or the genetic ablation of Apaf1 protects cells from apoptotic death. Moreover, we explored the function of two protein domains in LRRK2 (LRR and WD40) and demonstrate that the lack of these protein domains has a protective effect on mitochondria dysfunctions induced by mutant LRRK2.

© The Author 2007. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Topic:

• cell death
• phosphotransferases
• transfection
• apoptotic protease-activating factor 1
• lrrk2 gene

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