Post-translational modifications of Parkinson’s disease-related proteins: Phosphorylation, SUMOylation and Ubiquitination
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 2019-08-01; 1865(8): 2001-2007
DOI: 10.1016/j.bbadis.2018.10.025
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1. Biochim Biophys Acta Mol Basis Dis. 2019 Aug 1;1865(8):2001-2007. doi:
10.1016/j.bbadis.2018.10.025. Epub 2018 Nov 6.
Post-translational modifications of Parkinson’s disease-related proteins:
Phosphorylation, SUMOylation and Ubiquitination.
Junqueira SC(1), Centeno EGZ(1), Wilkinson KA(2), Cimarosti H(3).
Author information:
(1)Department of Pharmacology, Federal University of Santa Catarina,
Florianopolis, Brazil.
(2)School of Biochemistry, Centre for Synaptic Plasticity, University of
Bristol, Bristol, UK. Electronic address: .
(3)Department of Pharmacology, Federal University of Santa Catarina,
Florianopolis, Brazil. Electronic address: .
Parkinson’s disease (PD) is a neurodegenerative disorder characterized by loss
of dopaminergic neurons in the nigrostriatal pathway. The etiology of PD remains
unclear and most cases are sporadic, however genetic mutations in more than 20
proteins have been shown to cause inherited forms of PD. Many of these proteins
are linked to mitochondrial function, defects in which are a central
characteristic of PD. Post-translational modifications (PTMs) allow rapid and
reversible control over protein function. Largely focussing on mitochondrial
dysfunction in PD, here we review findings on the PTMs phosphorylation,
SUMOylation and ubiquitination that have been shown to affect PD-related
proteins.
Copyright © 2018 Elsevier B.V. All rights reserved.
DOI: 10.1016/j.bbadis.2018.10.025
PMID: 30412791 [Indexed for MEDLINE]