Document Type

Honors Project

Publication Date

6-13-2025

Abstract

Clathrin-mediated endocytosis (CME) is a cellular process for internalizing extracellular materials and recycling parts of the plasma membrane into intracellular vesicles. When a threshold of membrane-bound receptors is met at the cell surface, endocytic proteins organize into a conformation that can invaginate the membrane and separate a vesicle into the cytosol. Our current model for understanding CME has been derived from studies in Saccharomyces cerevisiae. Previous research has led to a model for how Las17, a homolog of Wiskott Aldrich Syndrome Protein (WASP), contributes to CME. WASP proteins are critical actin nucleators involved in multiple processes. In S. cerevisiae, Las17 is recruited to CME sites where it initiates rapid branched actin polymerization, and recruits type-1 myosins: Myo3 and Myo5. WASP coordination with Myo3/5 is required for endocytic invagination and abscission. We explore whether CME in other eukaryotic organisms follows the same mechanistic function as in S. cerevisiae. We assess how the S. cerevisiae model may work with a WASP homologous protein from an evolutionarily distinct relative, Schizosaccharomyces pombe. Using live-cell light microscopy, we quantify the relative recruitment of WASP homologs to the cortex and employ kymograph analysis to evaluate vesicle trafficking phenotypes. Our findings bridge the application of yeast CME to more complex eukaryotic endocytosis.

Level of Honors

magna cum laude

Department

Biology

Advisor

Alyssa Hakes, Eric Lewellyn

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