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Exploring the roles of Bzz1 in clathrin-mediated endocytosis

Date

2015

Authors

Barry, Lauren Marie, author
Di Pietro, Santiago, advisor
Curthoys, Norm, committee member
Glycenfer, Frances, committee member

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Abstract

Clathrin-mediated endocytosis (CME) is a highly conserved process in eukaryotes. This particular route of endocytosis plays an integral role in virus internalization, nutrient uptake, regulation of signal transduction, and overall cell health. CME can be characterized by three distinct stages: coat formation, cargo binds a receptor on the plasma membrane which leads to the recruitment of coat proteins and the formation of a clathrin coated pit; actin polymerization, globular actin will polymerize in such a way that the vesicle can overcome the turgor pressure of the plasma membrane; and scission and coat disassembly, the vesicle is separated from the plasma membrane and the coat proteins are recycled for the next endocytic event. Initiation of actin polymerization is mediated by the activation of the Arp2/3 complex. Arp2/3 is activated by Las17, the yeast homolog of human WASp (Wiskott-Aldrich Syndrome protein). Las17 interacts with multiple proteins, both activators and inhibitors. The activity of Las17 is inhibited by a protein called Sla1. Sla1 binds the P8-12 region of Las17 and blocks one of two globular actin binding sites. Sla1 and Las17 form a stable complex referred to as SLAC (Sla1, Las17, Actin, and Clathrin) and arrive at the plasma membrane together. This project deals specifically with the interaction between the SLAC complex and the putative activator Bzz1 and explores the possibility that Bzz1 both activates actin polymerization and tubulates the plasma membrane. Understanding the mechanisms that allow clathrin-mediated endocytosis to progress from start to finish is critical. Wiskott-Aldrich Syndrome, hypercholesterolemia, and neurodegenerative disorders can all be tied to defects in CME.

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Subject

Bzz1
Las17
actin polymerization
Sla1
clathrin-mediated endocytosis

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