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Role of the BAR domain proteins EndoA3 and PSTPIP1 in the clathrin-independent endocytosis of L1CAM

Ceuppens, Apolline
(2022)

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Details

Supervisors
Morsomme, Pierre ; Lemaigre, Camille
Faculty
Faculté des sciences
Degree label
Master [120] en biochimie et biologie moléculaire et cellulaire, à finalité approfondie
Abstract
Endocytosis is defined as a cellular mechanism that allows the internalization of molecules from the plasma membrane into the cytoplasm in small vesicles. This process is crucial for the cell physiology in many ways including nutrient uptake, cell signalling, cell adhesion and migration and membrane remodelling. Since the 2000’s, endocytic pathways diversity described in literature has grown rapidly. In addition to the well-known clathrin-mediated endocytosis, it is now known that there are several clathrin-independent endocytic mechanisms. Isoform 2 of L1 Cell Adhesion Molecule was recently identified in the laboratory as a new cargo from the clathrin-independent endocytosis. Since the associated roles of BAR domain proteins are to sense and/or induce membrane curvature, it was suspected that they may play an important role in the endocytic process. This was supported by data obtained last year by the previous master student (Bastien Vanbeneden) that identified the two BAR domain proteins EndoA3 and PSTPIP1 as probably involved. In the following master thesis, we confirmed EndoA3 and PSTPIP1 involvement in L1CAM endocytosis and we revealed how depletion of each BAR domain protein affects L1CAM endocytosis over time. In addition, we demonstrated that EndoA3 and PSTPIP1 may interact physically with L1CAM. Our data provide new insights in the field of endocytosis as it is the first time that PSTPIP1 is associated with endocytosis. In addition, it appears that EndoA3 may be involved in the uptake mechanism of two distinct proteins, as it was previously identified as being involved in CD166 uptake, also studied in the laboratory. Taken together, our data support the existence of a new EndoA3-dependent clathrin-independent mechanism. It remains to be clarified whether this mechanism is the same as that identified for CD166.

Citations

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Ceuppens, A. (2022). Role of the BAR domain proteins EndoA3 and PSTPIP1 in the clathrin-independent endocytosis of L1CAM. https://dial-mem.test.bib.ucl.ac.be/handle/2078.2/26788