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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 LU ; Zetterberg, Fredrik R. ; Nilsson, Ulf J LU ; Johannes, Ludger and Wunder, Christian , et al. (2023) In Traffic: the International Journal of Intracellular Transport 24(4). p.190-212
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... (More)

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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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Traffic: the International Journal of Intracellular Transport
volume
24
issue
4
pages
190 - 212
publisher
Wiley-Blackwell
external identifiers
  • pmid:36843549
  • scopus:85149742218
ISSN
1398-9219
DOI
10.1111/tra.12883
language
English
LU publication?
yes
additional info
This article is protected by copyright. All rights reserved.
id
212e073b-0103-4229-b3ec-6331ed9f8679
date added to LUP
2023-03-06 22:15:30
date last changed
2024-04-19 20:22:06
@article{212e073b-0103-4229-b3ec-6331ed9f8679,
  abstract     = {{<p>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.</p>}},
  author       = {{Lemaigre, Camille and Ceuppens, Apolline and Valades-Cruz, Cesar Augusto and Ledoux, Benjamin and Vanbeneden, Bastien and Hassan, Mujtaba and Zetterberg, Fredrik R. and Nilsson, Ulf J and Johannes, Ludger and Wunder, Christian and Renard, Henri-François and Morsomme, Pierre}},
  issn         = {{1398-9219}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{4}},
  pages        = {{190--212}},
  publisher    = {{Wiley-Blackwell}},
  series       = {{Traffic: the International Journal of Intracellular Transport}},
  title        = {{N-BAR and F-BAR proteins - Endophilin-A3 and PSTPIP1 - control clathrin-independent endocytosis of L1CAM}},
  url          = {{http://dx.doi.org/10.1111/tra.12883}},
  doi          = {{10.1111/tra.12883}},
  volume       = {{24}},
  year         = {{2023}},
}