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<span style="font-family: Tahoma, sans-serif; font-size: 38pt; color: rgb(255, 184, 27);"><b>Institute of Integrative Genome Biology Seminar</b></span></p>
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<span style="font-family: Tahoma, sans-serif; font-size: 20.5pt; color: rgb(0, 60, 165);"><b>You are cordially invited to attend:</b></span></p>
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<span style="font-family: "Book Antiqua", serif; font-size: 25pt;">Dani</span><span style="font-family: "Book Antiqua", serif; font-size: 25pt; color: rgb(0, 0, 0);">ë</span><span style="font-family: "Book Antiqua", serif; font-size: 25pt;">l Van Damme</span></p>
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<span style="font-family: Tahoma, sans-serif; font-size: 17.5pt; color: rgb(0, 74, 172);">VIB Center for Plant Systems Biology</span></p>
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<span style="color: rgb(0, 0, 0);"><img alt="Daniël Van Damme" id="image_0" width="365" height="365" style="width: 365px; height: 365px; margin-top: 0px; margin-bottom: 0px;" src="https://www.ugent.be/img/doza/portret/daniel-van-damme/@@images/9508917d-69e5-4cc2-b174-6a2c62b5cdef.jpeg"></span></p>
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<span style="font-size: 22pt; color: rgb(0, 74, 172); line-height: 116%;">Order and disorder in clathrin-mediated endocytosis in plants</span></p>
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Date: Friday, July 12, 2024</p>
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Time: 12:00 – 1:00 pm</p>
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Location: Genomics Auditorium 1102A</p>
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<p style="margin-top: 0px; margin-bottom: 0px;"><span style="font-size: 11pt;"><b>Abstract:</b>
</span><span style="font-family: "Times New Roman", serif; font-size: 11pt; color: rgb(0, 0, 0); font-weight: 400;">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.</span></p>
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<p style="margin: 0in; font-family: Aptos, sans-serif; font-size: 12pt;"><span style="font-size: 11pt;"> </span></p>
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