N-BAR and F-BAR proteins-endophilin-A3 and PSTPIP1-control clathrin-independent endocytosis of L1CAM.
Autor: | Lemaigre C; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium., Ceuppens A; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium., Valades-Cruz CA; Institut Curie, Université PSL, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, France.; SERPICO Project Team, UMR144 CNRS Institut Curie, PSL Research University, Paris, France.; SERPICO Project Team, Inria Centre Rennes-Bretagne Atlantique, Campus Universitaire de Beaulieu, Rennes, France., Ledoux B; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium., Vanbeneden B; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium., Hassan M; Department of Chemistry, Lund University, Lund, Sweden., Zetterberg FR; Galecto Biotech AB, Sahlgrenska Science Park, Gothenburg, Sweden., Nilsson UJ; Department of Chemistry, Lund University, Lund, Sweden., Johannes L; Institut Curie, Université PSL, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, France., Wunder C; Institut Curie, Université PSL, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, France., Renard HF; UNamur, NARILIS, Unité de recherche en biologie cellulaire animale (URBC), Namur, Belgium., Morsomme P; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium. |
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Jazyk: | angličtina |
Zdroj: | Traffic (Copenhagen, Denmark) [Traffic] 2023 Apr; Vol. 24 (4), pp. 190-212. |
DOI: | 10.1111/tra.12883 |
Abstrakt: | 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 clathrin-mediated 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. (© 2023 The Authors. Traffic published by John Wiley & Sons Ltd.) |
Databáze: | MEDLINE |
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