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Professor of BiochemistryProfessor of
Obstetrics and Gynecology
Primary Office: 3135E MERFIowa City, IA 52242
Email: email@example.comWeb: Geyer Laboratory
BS, McGill UniversityPhD, Ohio State University
Post Doctorate, Dept of Biology, Johns Hopkins UniversityPost Doctorate, Dept of Biology, Johns Hopkins University
Department of Biochemistry PhDInterdisciplinary Graduate Program in GeneticsInterdisciplinary Graduate Program in Molecular and Cellular BiologyInterdisciplinary Graduate Program in NeuroscienceInterdisciplinary Graduate Program in Translational BiomedicineMedical Scientist Training Program
The Geyer laboratory is interested in understanding mechanisms involved in genome organization and gene regulation. Two areas are currently being studied, insulators and nuclear lamina function. Insulators are a specialized class of DNA regulatory elements that have a conserved role in chromosome organization, dividing chromosomes into independent functional domains. These elements shelter genes from the surrounding positive and negative regulatory effects by blocking interactions between enhancers, silencers and promoters. Such properties have made insulators favorable candidates to improve strategies for gene therapy. While gene therapy is a promising technology that delivers therapeutic genes to a target tissue, successful application of this approach faces many challenges, including the cross regulation of endogenous genes by DNA regulatory elements in the vector. Insulators may prevent such undesirable effects. Studies in the Geyer lab include determination of the molecular mechanisms used by insulators to prevent interactions between enhancers, silencers and promoters and the identification of novel insulators. Combinations of insulators that employ different regulatory mechanisms may provide optimal protection of transgenes from the position effects of the surrounding chromatin and prevent sequences in the vector from mis-regulating endogenous genes at the site of genomic insertion. As such, insights into insulator mechanisms will allow advances in improving strategies for gene therapy and treatment of human disease. The nuclear lamina is an extensive protein network that lines the inner surface of the nuclear membrane. This network consists of intermediate filament proteins, called lamins, and associated inner nuclear membrane proteins, such as the LEM domain proteins. LEM domain genes make essential contributions to the function of the lamina, as mutations in these genes cause human diseases, known as laminopathies. For example, mutations in the genes that encode emerin and MAN1 cause Emery-Dreifuss Muscular Dystrophy and Buschke-Ollendorf Syndrome, respectively. Interestingly, these diseases are associated with tissue-specific pathologies, even though LEM domain genes are broadly expressed. To understand mechanisms underlying such human diseases, the Geyer lab is investigating the role of LEM domain proteins in lamina function, using Drosophila as a model organism. A molecular genetic approach is being taken to determine the contributions that individual LEM domain proteins make to nuclear lamina function.
Institute for Clinical and Translational Science
Unique and shared functions of nuclear lamina LEM domain proteins in Drosophila, Genetics accepted..
Genetics Society of America;
The insulator protein Suppressor of Hairy-wing is an essential transcriptional repressor in the Drosophila ovary.
2013 September. 140(17):3613-23.
The Drosophila nuclear lamina protein otefin is required for germline stem cell survival.
2013 June. 25(6):645-54.
Restoration of topoisomerase 2 function by complementation of defective monomers in Drosophila.
2012 November. 192(3):843-56.
Genome-wide studies of the multi-zinc finger Drosophila Suppressor of Hairy-wing protein in the ovary.
Nucleic Acids Research .
2012 July. 40(12).
The role of the Suppressor of Hairy-wing insulator protein in Drosophila oogenesis.
2011 August. 356(2):398-410.
Nuclear organization: taking a position on gene expression.
Current opinion in cell biology.
2011 June. 23(3):354-9.
The role of Drosophila Lamin C in muscle function and gene expression.
Development (Cambridge, England).
2010 September. 137(18):3067-77.
A comparative study of Drosophila and human A-type lamins.
Tissue-specific defects are caused by loss of the Drosophila MAN1 LEM domain protein.
2008 September. 180(1):133-45.
Date Last Modified: 10/09/2015 -
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