Regulated EMRE protein level in the Mitochondrial Calcium Uniporter

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dc.contributor.advisor Miller, Christopher
dc.contributor.author Wu, Yujiao Jr
dc.date.accessioned 2016-04-26T20:04:28Z
dc.date.available 2016-04-26T20:04:28Z
dc.date.issued 2016
dc.identifier.uri http://hdl.handle.net/10192/32107
dc.description.abstract Mitochondrial Calcium Uniporter serves as the major portal for calcium influx into the matrix. It is a highly regulated ion channel complex composed of the pore forming subunit MCU and multiple regulatory subunits, among which the Essential MCU REgulator (EMRE) is necessary for the calcium conducting function of MCU. The goal of this work is to understand how cells regulate EMRE expression level. Using a cycloheximide chase assay, I found that MCU protects EMRE from rapid proteolysis by the mitochondrial m-AAA (ATPases Associated with diverse cellular Activities) protease. Experiments show that such protection requires interactions between the two proteins’ transmembrane helices (TMHs). Then I use EMRE homologues and chimeras to show that the rate-limiting step for EMRE degradation occurs after initial protease binding to the EMRE’s N-terminus. This work revealed a post-translational mechanism by which balanced expression of uniporter subunits is achieved, a condition that might be crucial for proper assembly of the uniporter complex.
dc.description.sponsorship Brandeis University, Graduate School of Arts and Sciences
dc.format.mimetype application/pdf
dc.language English
dc.language.iso eng
dc.publisher Brandeis University
dc.relation.ispartofseries Brandeis University Theses and Dissertations
dc.rights Copyright by Yujiao Wu 2016
dc.subject Mitochondrial Calcium Uniporter
dc.subject EMRE
dc.subject m-AAA protease
dc.subject quality control
dc.title Regulated EMRE protein level in the Mitochondrial Calcium Uniporter
dc.type Thesis
dc.contributor.department Department of Biochemistry
dc.degree.name MS
dc.degree.level Masters
dc.degree.discipline Biochemistry
dc.degree.grantor Brandeis University, Graduate School of Arts and Sciences


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