GSBS Dissertations and Theses

Approval Date

10-28-2015

Document Type

Doctoral Dissertation

Academic Program

Cell Biology

Department

Biochemistry and Molecular Pharmacology

First Thesis Advisor

Anthony N. Imbalzano, PhD

Keywords

Adipocytes, Cell Differentiation, Gene Expression Regulation, Protein-Arginine N-Methyltransferases, Jumonji Domain-Containing Histone Demethylases

Subjects

Dissertations, UMMS; Adipocytes; Cell Differentiation; Gene Expression Regulation; Protein-Arginine N-Methyltransferases; Jumonji Domain-Containing Histone Demethylases

Abstract

Regulation of gene expression comprises a wide range of mechanisms that control the abundance of gene products in response to environmental and developmental changes. These biological processes can be modulated by posttranslational modifications including arginine methylation. Among the enzymes that catalyze the methylation, protein arginine methyltransferase 7 (PRMT7) is known to modify histones to repress gene expression. Jumonji domain-containing protein 6 (JMJD6) is a putative arginine demethylase that potentially antagonize PRMT7. However, the biological significance of these enzymes is not well understood. This thesis summarizes the investigation of both PRMT7 and JMJD6 in cell culture models for adipocyte differentiation. The results suggest that PRMT7 is not required for the differentiation, whereas JMJD6 is necessary for the differentiation by promoting the expression of the lineage determining transcription factors peroxisome proliferator-activated receptor γ (PPARγ) and CCAAT/enhancerbinding proteins (C/EBPs). The underlying mechanisms by which JMJD6 regulate differentiation involve transcriptional and post-transcriptional control of gene expression. Unexpectedly, the adipogenic function of JMJD6 is independent of its enzymatic activity. Collectively, the present research reveals a novel role of JMJD6 in gene regulation during the differentiation of adipocytes.

DOI

10.13028/M2R300

Rights and Permissions

Copyright is held by the author, with all rights reserved.

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