Liquid-liquid phase separation and extracellular multivalent interactions in the tale of galectin-3

Yi-Ping Chiu, Yung-Chen Sun, Qiu De-Chen, Yu-Hao Lin, Yin-Quan Chen, Jean-Cheng Kuo and Jie-rong Huang ()
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Yi-Ping Chiu: National Yang-Ming University
Yung-Chen Sun: National Yang-Ming University
Qiu De-Chen: National Yang-Ming University
Yu-Hao Lin: National Yang-Ming University
Yin-Quan Chen: National Yang-Ming University
Jean-Cheng Kuo: National Yang-Ming University
Jie-rong Huang: National Yang-Ming University

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract Liquid-liquid phase separation (LLPS) explains many intracellular activities, but its role in extracellular functions has not been studied to the same extent. Here we report how LLPS mediates the extracellular function of galectin-3, the only monomeric member of the galectin family. The mechanism through which galectin-3 agglutinates (acting as a “bridge” to aggregate glycosylated molecules) is largely unknown. Our data show that its N-terminal domain (NTD) undergoes LLPS driven by interactions between its aromatic residues (two tryptophans and 10 tyrosines). Our lipopolysaccharide (LPS) micelle model shows that the NTDs form multiple weak interactions to other galectin-3 and then aggregate LPS micelles. Aggregation is reversed when interactions between the LPS and the carbohydrate recognition domains are blocked by lactose. The proposed mechanism explains many of galectin-3’s functions and suggests that the aromatic residues in the NTD are interesting drug design targets.

Date: 2020
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DOI: 10.1038/s41467-020-15007-3

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