Alpha-synuclein knockout impairs melanoma development and alters DNA damage repair in the TG3 mouse model in a sex-dependent manner.

Strong evidence suggests links between Parkinson's Disease (PD) and melanoma, as studies have found that people with PD are at an increased risk of developing melanoma and those with melanoma are at increased risk of developing PD. Although these clinical associations are well-established, the cellular and molecular pathways linking these diseases are poorly understood. Recent studies have found a previously unrecognized role for the neurodegeneration-associated protein alpha-synuclein (αSyn) in melanoma; the overexpression of αSyn promotes melanoma cell proliferation and metastasis.

Polo-like kinase inhibition leads to neuroprotection of neurons bearing alpha-synuclein Lewy body-like inclusions .

α-synuclein (αSyn) and S129 phosphorylated αSyn (pSyn) define synucleinopathies like Parkinson's disease (PD). Targeting S129 αSyn kinases, like the Polo-like kinase (PLK) family, could provide a therapeutic strategy to limit degeneration of cells bearing aggregated αSyn inclusions. Using longitudinal multiphoton imaging in mouse cortex after αSyn inclusion induction, we find an increase in cell survival of inclusion-bearing neurons after PLK inhibition.

Community structure of tropics emerging from spatio-temporal variations in the Intertropical Convergence Zone dynamics.

The Intertropical Convergence Zone (ITCZ) is a narrow tropical belt of deep convective clouds, intense precipitation, and monsoon circulations encircling the Earth. Complex interactions between the ITCZ and local geophysical dynamics result in high climate variability, making weather forecasting and prediction of extreme rainfall or drought events challenging. We unravel the complex spatio-temporal dynamics of the ITCZ and the resulting teleconnection patterns via a novel tropical climate classification achieved using complex network analysis and community detection.

Alpha-synuclein modulates the repair of genomic DNA double-strand breaks in a DNA-PK-regulated manner.

α-synuclein (αSyn) is a presynaptic and nuclear protein that aggregates in important neurodegenerative diseases such as Parkinson's Disease (PD), Parkinson's Disease Dementia (PDD) and Lewy Body Dementia (LBD). Our past work suggests that nuclear αSyn may regulate forms of DNA double-strand break (DSB) repair in HAP1 cells after DNA damage induction with the chemotherapeutic agent bleomycin. Here, we report that genetic deletion of αSyn specifically impairs the non-homologous end-joining (NHEJ) pathway of DSB repair using an extrachromosomal plasmid-based repair assay in HAP1 cells.

Aquaporin-4 mis-localization slows glymphatic clearance of α-synuclein and promotes α-synuclein pathology and aggregate propagation.

The appearance of misfolded and aggregated proteins is a pathological hallmark of numerous neurodegenerative diseases including Alzheimer's disease and Parkinson's disease. Sleep disruption is proposed to contribute to these pathological processes and is a common early feature among neurodegenerative disorders. Synucleinopathies are a subclass of neurodegenerative conditions defined by the presence of α-synuclein aggregates, which may not only enhance cell death, but also contribute to disease progression by seeding the formation of additional aggregates in neighboring cells.