N-BAR and F-BAR proteins—endophilin-A3 and PSTPIP1—control clathrin-independent endocytosis of L1CAM
(2023) Traffic : the international journal of intracellular transport — Vol. 24, n° 4, p. 190-212 (2023)
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Lemaigre, Camille 
- Abstract
- Recent advances in the field demonstrate the high diversity and complexity of endocytic pathways. In the current study, we focus on the endocytosis of L1CAM. This glycoprotein plays a major role in the development of the nervous system, and is involved in cancer development and is associated with metastases and poor prognosis. Two L1CAM isoforms are subject to endocytosis: isoform 1, described as a clathrinmediated cargo; isoform 2, whose endocytosis has never been studied. Deciphering the molecular machinery of isoform 2 internalisation should contribute to a better understanding of its pathophysiological role. First, we demonstrated in our cellular context that both isoforms of L1CAM are mainly a clathrin-independent cargo, which was not expected for isoform 1. Second, the mechanism of L1CAM endocytosis is specifically mediated by the N-BAR domain protein endophilin-A3. Third, we discovered PSTPIP1, an F-BAR domain protein, as a novel actor in this endocytic process. Finally, we identified galectins as endocytic partners and negative regulators of L1CAM endocytosis. In summary, the interplay of the BAR proteins endophilin-A3 and PSTPIP1, and galectins fine tune the clathrin-independent endocytosis of L1CAM.
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Lemaigre, C., Ceuppens, A., Valades‐Cruz, C. A., Ledoux, B., Vanbeneden, B., Hassan, M., Zetterberg, F. R., Nilsson, U. J., Johannes, L., Wunder, C., Renard, H.-F., & Morsomme, P. (2023). N-BAR and F-BAR proteins—endophilin-A3 and PSTPIP1—control clathrin-independent endocytosis of L1CAM. Traffic : the international journal of intracellular transport, 24(4), 190-212. https://doi.org/10.1111/tra.12883 (Original work published 2023)