SH3 domain-mediated assembly regulation of the endocytic machinery in yeast

Diplôme Thèse SH3 domain-mediated assembly regulation of the endocytic machinery in yeast eng 2022-02-09 2022-02-15 author Hummel Daniel 865462 director Kaksonen Marko 0000-0003-3645-7689 830048 10.13097/archive-ouverte/unige:160126 urn:nbn:ch:unige-1601269 Sc. Vie 147 Clathrin-mediated endocytosis (CME) is a conserved Eukaryotic trafficking pathway that is driven by a sequentially self-assembled molecular machinery of over 50 different proteins. What protein-protein interactions regulate assembly of the endocytic machinery? I describe how the most abundant PPI domain family in CME – SH3 domains – regulate endocytic protein assembly in the budding yeast Saccharomyces cerevisiae, combining mutagenesis with live cell fluorescence microscopy. My data suggest that most SH3 domains regulate recruitment of their own SH3 protein and SH3 domains that recruit other endocytic proteins do not promote recruitment of their own SH3 protein. Furthermore, multiple SH3 domains mediate the same endocytic component, the Las17/Vrp1 complex (LVC), and interfere with each other. The SH3 interaction network coordinates LVC assembly and dissociation dynamics. My results provide a dynamic map of SH3 functions in yeast endocytosis that can help SH3 research in a broad biological and medical context to conceptualize SH3 interaction networks. Dewey 500 2 Faculté des sciences 1 false 3e6c4ea7-dcc6-47da-95b2-026fa8328304 Thesis Restricted Daniel_Hummel_PhD_Thesis_print.pdf 4249816 application/pdf 4e030a282e530e64d13437c0ac6b09de0d9e732aec2bce431596043b3461caec 1aeff142-4ff0-41b5-8f19-207d4e174f1f Agreement Private Hummel-Daniel_Contrat_diffusion_the.pdf 500045 application/pdf 811ee28e-6002-49bb-a25d-8d73d53888af Publication mode Private Hummel-Daniel_Mode-de-publication.pdf 1315500 application/pdf restrictedAccess Faculté des sciences

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SH3 domain-mediated assembly regulation of the endocytic machinery in yeast				2022	417	10

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