Next Article in Journal
Protein Binding to Cis-Motifs in mRNAs Coding Sequence Is Common and Regulates Transcript Stability and the Rate of Translation
Previous Article in Journal
Novel Peptide Therapeutic Approaches for Cancer Treatment
Article

Anti-Aggregative Effect of the Antioxidant DJ-1 on the TPPP/p25-Derived Pathological Associations of Alpha-Synuclein

Cell Architecture Lab, Research Center for Natural Sciences, Institute of Enzymology, 1117 Budapest, Hungary
*
Authors to whom correspondence should be addressed.
Academic Editor: Cristine Alves Da Costa
Cells 2021, 10(11), 2909; https://doi.org/10.3390/cells10112909
Received: 10 September 2021 / Revised: 22 October 2021 / Accepted: 25 October 2021 / Published: 27 October 2021
DJ-1, a multi-functional protein with antioxidant properties, protects dopaminergic neurons against Parkinson’s disease (PD). The oligomerization/assembly of alpha-synuclein (SYN), promoted by Tubulin Polymerization Promoting Protein (TPPP/p25), is fatal in the early stage of PD. The pathological assembly of SYN with TPPP/p25 inhibits their proteolytic degradation. In this work, we identified DJ-1 as a new interactive partner of TPPP/p25, and revealed its influence on the association of TPPP/p25 with SYN. DJ-1 did not affect the TPPP/p25-derived tubulin polymerization; however, it did impede the toxic assembly of TPPP/p25 with SYN. The interaction of DJ-1 with TPPP/p25 was visualized in living human cells by fluorescence confocal microscopy coupled with Bifunctional Fluorescence Complementation (BiFC). While the transfected DJ-1 displayed homogeneous intracellular distribution, the TPPP/p25-DJ-1 complex was aligned along the microtubule network. The anti-aggregative effect of DJ-1 on the pathological TPPP/p25-SYN assemblies was established by the decrease in the intensity of their intracellular fluorescence (BiFC signal) and the increase in the proteolytic degradation of SYN complexed with TPPP/p25 due to the DJ-1-derived disassembly of SYN with TPPP/p25. These data obtained with HeLa and SH-SY5Y cells revealed the protective effect of DJ-1 against toxic SYN assemblies, which assigns a new function to the antioxidant sensor DJ-1. View Full-Text
Keywords: alpha-synuclein; TPPP/p25; DJ-1; parkinsonism; anti-aggregative effect; BiFC alpha-synuclein; TPPP/p25; DJ-1; parkinsonism; anti-aggregative effect; BiFC
Show Figures

Figure 1

MDPI and ACS Style

Oláh, J.; Lehotzky, A.; Szénási, T.; Ovádi, J. Anti-Aggregative Effect of the Antioxidant DJ-1 on the TPPP/p25-Derived Pathological Associations of Alpha-Synuclein. Cells 2021, 10, 2909. https://doi.org/10.3390/cells10112909

AMA Style

Oláh J, Lehotzky A, Szénási T, Ovádi J. Anti-Aggregative Effect of the Antioxidant DJ-1 on the TPPP/p25-Derived Pathological Associations of Alpha-Synuclein. Cells. 2021; 10(11):2909. https://doi.org/10.3390/cells10112909

Chicago/Turabian Style

Oláh, Judit, Attila Lehotzky, Tibor Szénási, and Judit Ovádi. 2021. "Anti-Aggregative Effect of the Antioxidant DJ-1 on the TPPP/p25-Derived Pathological Associations of Alpha-Synuclein" Cells 10, no. 11: 2909. https://doi.org/10.3390/cells10112909

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop