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Updated: Feb 18, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
Published on: November 25, 2022
Interaction of Alpha-synuclein with Cytogaligin, a protein encoded by the proapoptotic gene GALIG
Saïd El Haddad1, Amandine Serrano1, Thierry Normand1
1Centre de Biophysique Moléculaire, CNRS UPR 4301, Affiliated with the Université d'Orléans - Pôle Universitaire Centre Val de Loire, Rue Charles Sadron, 45071 Orléans Cedex 2, France.
Abstract:
GALIG, an internal gene to the human galectin-3 gene, encodes two distinct proteins, Mitogaligin and Cytogaligin through translation of a unique mRNA in two overlapping alternative reading frames. When overexpressed GALIG induces apoptosis. In cultured cells, Mitogaligin destabilizes mitochondria membranes through interaction with cardiolipin. Little is known regarding the role of Cytogaligin. This protein displays multiple subcellular localizations; cytosol, nucleus, and mitochondria. We illustrate here that Cytogaligin is also secreted in the extracellular medium. Cytogaligin is shown to interact with α-Synuclein, the major component of Lewy bodies in Parkinson's disease. Overexpression of Cytogaligin reduces α-Synuclein dimerization raising a possible role in the evolution of α-Synuclein aggregation, a key molecular event underlying the pathogenesis of Parkinson's disease.
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