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STUDIES ON E2 CONJUGATION ENZYME PARTNERS OF MULAN E3 UBIQUITIN LIGASE

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Date Issued:
2018
Abstract/Description:
Mulan is an E3 ubiquitin ligase embedded in the outer mitochondria membrane. Mulan's participation in the ubiquitination process is conducted through its cytosol exposed RING finger domain, and its ability to modulate protein ubiquitination makes it a key player in mitochondrial and cellular homeostasis. Mulan is known to be involved in mitochondrial fission, fusion, mitochondrial stress, apoptosis, and Parkin-independent mitophagy. Dysregulation of Mulan in mice has been shown to correlate with human neurodegenerative disorders and heart disease. Accumulation of Mulan is predicted to be responsible for the motor neuron degeneration 2 (mnd2) phenotype in mutant mice through the deregulation of the Mulan-dependent pathway of mitophagy. The purpose of this study was to utilize both a yeast two-hybrid screen as well as an in vitro profiling assay to characterize interactions between Mulan and potential E2 conjugating enzymes. Through these studies, Ube2D1, Ube2D2, and Ube2D3 were identified as strong interactors with the Mulan-RING domain. The tissue specific expression and protein levels of these E2 conjugating enzymes was further investigated in mouse tissues by SDS-PAGE and Western blot analysis. They all had similar patterns of expression and were present in brain, heart, kidney, and liver tissues, with the highest level seen in the brain. This data demonstrates that Mulan has a primary function in the brain and it suggests that Mulan's deregulation might be involved in the development and progression of neurodegeneration.
Title: STUDIES ON E2 CONJUGATION ENZYME PARTNERS OF MULAN E3 UBIQUITIN LIGASE.
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Name(s): Fitzpatrick, Rebekah J, Author
Zervos, Antonis S., Committee Chair
University of Central Florida, Degree Grantor
Type of Resource: text
Date Issued: 2018
Publisher: University of Central Florida
Language(s): English
Abstract/Description: Mulan is an E3 ubiquitin ligase embedded in the outer mitochondria membrane. Mulan's participation in the ubiquitination process is conducted through its cytosol exposed RING finger domain, and its ability to modulate protein ubiquitination makes it a key player in mitochondrial and cellular homeostasis. Mulan is known to be involved in mitochondrial fission, fusion, mitochondrial stress, apoptosis, and Parkin-independent mitophagy. Dysregulation of Mulan in mice has been shown to correlate with human neurodegenerative disorders and heart disease. Accumulation of Mulan is predicted to be responsible for the motor neuron degeneration 2 (mnd2) phenotype in mutant mice through the deregulation of the Mulan-dependent pathway of mitophagy. The purpose of this study was to utilize both a yeast two-hybrid screen as well as an in vitro profiling assay to characterize interactions between Mulan and potential E2 conjugating enzymes. Through these studies, Ube2D1, Ube2D2, and Ube2D3 were identified as strong interactors with the Mulan-RING domain. The tissue specific expression and protein levels of these E2 conjugating enzymes was further investigated in mouse tissues by SDS-PAGE and Western blot analysis. They all had similar patterns of expression and were present in brain, heart, kidney, and liver tissues, with the highest level seen in the brain. This data demonstrates that Mulan has a primary function in the brain and it suggests that Mulan's deregulation might be involved in the development and progression of neurodegeneration.
Identifier: CFH2000305 (IID), ucf:45920 (fedora)
Note(s): 2018-05-01
B.S.
College of Medicine, Burnett School of Biomedical Sciences
Bachelors
This record was generated from author submitted information.
Subject(s): Mulan
mitochondria
mitophagy
Ube2D1
Ube2D2
Ube2D3
Persistent Link to This Record: http://purl.flvc.org/ucf/fd/CFH2000305
Restrictions on Access: campus 2019-05-01
Host Institution: UCF

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