TY  - JOUR
AU  - Defelipe, Lucas A.
AU  - Veith, Katharina
AU  - Burastero, Osvaldo
AU  - Kupriianova, Tatiana
AU  - Bento, Isabel
AU  - Skruzny, Michal
AU  - Koelbel, Knut
AU  - Uetrecht, Charlotte
AU  - Thuenauer, Roland
AU  - García-Alai, Maria M.
TI  - Subtleties in Clathrin heavy chain binding boxes provide selectivity among adaptor proteins of budding yeast
JO  - Nature Communications
VL  - 15
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Nature Publishing Group UK
M1  - PUBDB-2024-08038
SP  - 9655
PY  - 2024
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:39511183
UR  - <Go to ISI:>//WOS:001352440200007
DO  - DOI:10.1038/s41467-024-54037-z
UR  - https://bib-pubdb1.desy.de/record/619947
ER  -