Protein polymers play essential roles in cell biology. In response to diverse events, cytosolic proteins can assemble into filaments with a range of properties. The foci of this dissertation are two different kinds of multicomponent filaments. In the first section, I describe a filamentous assembly of dynamin1 and endophilinA1 and the roles these proteins play during endocytosis. The second section concerns a copolymer that comprises Increased Sodium Tolerance 1 (IST1) with CHarged Multivesicular Body Protein 1B (CHMP1B) and the distinct roles of this coassembly on endosomal membranes and on exposed DNA present during the cell cycle. I employed biochemical, structural, and cell biological approaches to investigate how these proteins copolymerize and the functional properties of their resulting filaments. The dissertation concludes with key mechanistic insights into the features of these filaments and predicts that membrane-remodeling proteins may also serve as nucleic acid-binding or cytoskeleton-binding proteins by exploiting surfaces common to both processes.
|Commitee:||Hill, Christopher P., Rutter, Jared, Shaw, Janet, Babst, Markus|
|School:||The University of Utah|
|School Location:||United States -- Utah|
|Source:||DAI-B 81/8(E), Dissertation Abstracts International|
|Keywords:||CHMP1B, Cryo-EM, Dynamin, Endophilin, IST1, Membrane|
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