Subtleties in Clathrin heavy chain binding boxes provide selectivity among adaptor proteins of budding yeast

Lucas A. Defelipe, Katharina Veith, Osvaldo Burastero, Tatiana Kupriianova, Isabel Bento, Michal Skruzny, Knut Kölbel, Charlotte Uetrecht, Roland Thuenauer and Maria M. García-Alai ()
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Lucas A. Defelipe: European Molecular Biology Laboratory - Hamburg Unit
Katharina Veith: European Molecular Biology Laboratory - Hamburg Unit
Osvaldo Burastero: European Molecular Biology Laboratory - Hamburg Unit
Tatiana Kupriianova: European Molecular Biology Laboratory - Hamburg Unit
Isabel Bento: European Molecular Biology Laboratory - Hamburg Unit
Michal Skruzny: European Molecular Biology Laboratory
Knut Kölbel: Centre for Structural Systems Biology
Charlotte Uetrecht: Centre for Structural Systems Biology
Roland Thuenauer: Centre for Structural Systems Biology
Maria M. García-Alai: European Molecular Biology Laboratory - Hamburg Unit

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract Clathrin forms a triskelion, or three-legged, network that regulates cellular processes by facilitating cargo internalization and trafficking in eukaryotes. Its N-terminal domain is crucial for interacting with adaptor proteins, which link clathrin to the membrane and engage with specific cargo. The N-terminal domain contains up to four adaptor-binding sites, though their role in preferential occupancy by adaptor proteins remains unclear. In this study, we examine the binding hierarchy of adaptors for clathrin, using integrative biophysical and structural approaches, along with in vivo functional experiments. We find that yeast epsin Ent5 has the highest affinity for clathrin, highlighting its key role in cellular trafficking. Epsins Ent1 and Ent2, crucial for endocytosis but thought to have redundant functions, show distinct binding patterns. Ent1 exhibits stronger interactions with clathrin than Ent2, suggesting a functional divergence toward actin binding. These results offer molecular insights into adaptor protein selectivity, suggesting they competitively bind clathrin while also targeting three different clathrin sites.

Date: 2024
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DOI: 10.1038/s41467-024-54037-z

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