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N-BAR and F-BAR proteins-endophilin-A3 and PSTPIP1-control clathrin-independent endocytosis of L1CAM.
Lemaigre, Camille; Ceuppens, Apolline; Valades-Cruz, Cesar Augusto; Ledoux, Benjamin; Vanbeneden, Bastien; Hassan, Mujtaba; Zetterberg, Fredrik R; Nilsson, Ulf J; Johannes, Ludger; Wunder, Christian; Renard, Henri-François; Morsomme, Pierre.
  • 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.
  • Ledoux B; SERPICO Project Team, UMR144 CNRS Institut Curie, PSL Research University, Paris, France.
  • Vanbeneden B; SERPICO Project Team, Inria Centre Rennes-Bretagne Atlantique, Campus Universitaire de Beaulieu, Rennes, France.
  • Hassan M; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium.
  • Zetterberg FR; UCLouvain, Louvain Institute of Biomolecular Science and Technology, Group of Molecular Physiology, Louvain-la-Neuve, Belgium.
  • Nilsson UJ; Department of Chemistry, Lund University, Lund, Sweden.
  • Johannes L; Galecto Biotech AB, Sahlgrenska Science Park, Gothenburg, Sweden.
  • Wunder C; Department of Chemistry, Lund University, Lund, Sweden.
  • Renard HF; Institut Curie, Université PSL, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, France.
  • Morsomme P; Institut Curie, Université PSL, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, France.
Traffic ; 24(4): 190-212, 2023 04.
Article en En | MEDLINE | ID: mdl-36843549
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 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.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Clatrina / Molécula L1 de Adhesión de Célula Nerviosa Tipo de estudio: Prognostic_studies Idioma: En Año: 2023 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Clatrina / Molécula L1 de Adhesión de Célula Nerviosa Tipo de estudio: Prognostic_studies Idioma: En Año: 2023 Tipo del documento: Article