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Exploring the roles of Bzz1 in clathrin-mediated endocytosis

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dc.contributor.authorBarry, Lauren Marie, author
dc.contributor.authorDi Pietro, Santiago, advisor
dc.contributor.authorCurthoys, Norm, committee member
dc.contributor.authorGlycenfer, Frances, committee member
dc.date.accessioned2015-08-27T03:57:17Z
dc.date.available2016-06-03T03:56:54Z
dc.date.issued2015
dc.description.abstractClathrin-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.
dc.format.mediumborn digital
dc.format.mediummasters theses
dc.identifier.urihttp://hdl.handle.net/10217/166988
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.subjectBzz1
dc.subjectLas17
dc.subjectactin polymerization
dc.subjectSla1
dc.subjectclathrin-mediated endocytosis
dc.titleExploring the roles of Bzz1 in clathrin-mediated endocytosis
dc.typeText
dcterms.embargo.expires2016-06-03
dcterms.embargo.terms2016-06-03
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineBiochemistry and Molecular Biology
thesis.degree.grantorColorado State University
thesis.degree.levelMasters
thesis.degree.nameMaster of Science (M.S.)

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