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Endocytosis is crucial for various physiological processes, facilitating the uptake of membrane proteins and extracellular material. Fast endophilin-mediated endocytosis (FEME), driven by endophilin A (EndoA), enables clathrin-independent, ligand-induced receptor uptake at the leading edge of cells. Whilst F-actin polymerisation is essential for FEME, how actin dynamics are regulated at sites of FEME is unknown. NHSL1, a member of the Nance-Horan Syndrome protein family, localises to the leading edge of cells, where it regulates migration, and to vesicular puncta, where its function is undetermined. Here, we show that NHSL1 and its uncharacterised family member NHSL2 co-localise and engage in direct, multivalent interactions with EndoA. NHSL1 also binds Ena/VASP proteins, a family of actin elongators. NHSL1 promotes FEME in cells and its interactions with EndoA and Ena/VASP proteins are required for this function. Thus, NHSL1 may cooperate with EndoA and Ena/VASP proteins to control membrane invagination and actin polymerisation, thereby mediating FEME. ### Competing Interest Statement The authors have declared no competing interest.

The Idea of Moral Socialism event page

In this immersive portrait of play, children transform the streets of Havana into a racetrack with handmade ‘chivichanas’

Modelling the tumour immune microenvironment in vitro is a valuable tool to test immunotherapy efficiency but capturing its complexity is challenging. Here authors present a fully humanised in vitro p...

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