[CEPCEB_All] IIGB Seminar Notice: Daniel Van Damme 7/12/2024

[Mauricio Macias-Serrano]

Institute of Integrative Genome Biology Seminar

You are cordially invited to attend:

Daniël Van Damme

VIB Center for Plant Systems Biology

[Daniël Van Damme]

Order and disorder in clathrin-mediated endocytosis in plants

Date: Friday, July 12, 2024

Time: 12:00 – 1:00 pm

Location: Genomics Auditorium 1102A

Abstract: Endocytosis is essential to maintain plasma membrane proteome homeostasis. It does so by vesicle-mediated internalization, whose predominant mode of operation utilizes the scaffolding protein clathrin to coat the forming vesicles. The process therefore is termed clathrin-mediated endocytosis (CME). Throughout eukaryotic evolution, the machinery that mediates CME is marked by losses, multiplications and innovations. CME employs a limited number of conserved structural domains and folds, which are assembled and connected differently depending on the species. In plants, many of the domains are grouped into an ancient octameric protein complex, the TPLATE complex, which occupies a central position as an interaction hub for the endocytic machinery. The TPLATE adaptor complex (TPC) has been established as crucial for the execution of endocytosis in Arabidopsis. How this complex mechanistically functions to execute plant CME and how its function is connected to that of the other endocytic adaptor complex, AP-2, are active areas of research. Over the last couple of years, a multidisciplinary approach has provided us with insight into the structural composition as well as functional insight on some of the conserved domains that are grouped by this complex. We recently characterized some of its evolutionary adaptations and found that these subunits modulate endocytic dynamics as well as clathrin recruitment via the material properties of their intrinsically disordered domains that drive condensate formation of the TPC. Finally, our integrated structural model revealed that the detailed lipid binding capacities and domain organization of TPC both contribute to its membrane bending capacity during clathrin-coated vesicle formation.


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