Dr. Türker graduated as valedictorian with a B.Sc. in Molecular Biology, Genetics, and Bioengineering, and a minor in Chemistry, from Sabanci University in Turkey in 2017. During her undergraduate studies, she spent a semester as an exchange student at Boston University and interning at Harvard Medical School. She then pursued her Ph.D. in the Department of Biological Chemistry at Johns Hopkins University School of Medicine, US under the mentorship of Dr. Seth S. Margolis. Her dissertation focuses on identifying neuronal membrane proteasome-derived peptides with signaling capabilities in the mammalian nervous system. After earning her Ph.D., Dr. Türker joined Dr. Sandra Encalada's research group at The Scripps Research Institute, US as a postdoctoral research fellow. During her postdoctoral training, she was awarded the George E. Hewitt Foundation Fellowship. She is currently an Assistant Professor at the Molecular Biology and Genetics Department at Bilkent University, Turkey.
EDUCATION
2017 - 2023 Johns Hopkins University School of Medicine, MD, USA
Ph.D., Department of Biological Chemistry
2013 - 2017 Sabanci University, Istanbul, TURKEY
B.Sc., Department of Biological Sciences and Bioengineering
Minor Program: Chemistry
2016 Spring Boston University, MA, USA
Educational Abroad Program (Exchange student)
RESEARCH, TEACHING, or OTHER INTERESTS
Cellular and Molecular Neuroscience, Cell Biology, Molecular Biology, Biochemistry, Genetics and Molecular Biology
Neuronal membrane proteasome-derived peptides modulate NMDAR-dependent neuronal signaling to promote changes in gene expression Fulya Türker, Anna Brennan, Seth S. Margolis Molecular Biology of the Cell, 2024 The neuronal membrane proteasome (NMP) degrades intracellular proteins into peptides that are released directly into the extracellular space, whereby they stimulate neurons to promote signaling mechanisms that remain unknown. Here, we demonstrate that neuronal stimulation promotes NMP activity and, subsequently, enhanced production of NMP peptides. We show that these neuronal activity-dependent NMP peptides can rapidly promote N-methyl-D-aspartate receptor (NMDAR)-dependent calcium influx in neurons. This leads to sustained phosphorylation of the well-defined stimulus-induced transcription factor, cyclic AMP response element (CRE)-binding protein (CREB). Downstream of these events, we identified changes to neuronal target genes which included increased expression of immediate early genes (e.g., Fos, Npas4, Egr4) and other genes known to have critical neuroregulatory roles. Further observations led to the discovery that NMP peptide-induced changes in gene expression is dependent on NMDARs and independent of AMPA receptors or voltage-gated sodium channels. These data demonstrate that NMP peptides are endogenous and selective activators of NMDA receptors and act as sufficient and novel stimuli within the context of neuronal activity-dependent signaling. This novel pathway is parallel to classic neuronal activity-dependent programs and points to NMP and its resulting peptides as potential modulators of neuronal function.
Targeted DNA methylation in human cells using engineered dCas9-methyltransferases Tina Xiong, Glenna E. Meister, Rachael E. Workman, Nathaniel C. Kato, Michael J. Spellberg, et al. Scientific Reports, 2017 Mammalian genomes exhibit complex patterns of gene expression regulated, in part, by DNA methylation. The advent of engineered DNA methyltransferases (MTases) to target DNA methylation to specific sites in the genome will accelerate many areas of biological research. However, targeted MTases require clear design rules to direct site-specific DNA methylation and minimize the unintended effects of off-target DNA methylation. Here we report a targeted MTase composed of an artificially split CpG MTase (sMTase) with one fragment fused to a catalytically-inactive Cas9 (dCas9) that directs the functional assembly of sMTase fragments at the targeted CpG site. We precisely map RNA-programmed DNA methylation to targeted CpG sites as a function of distance and orientation from the protospacer adjacent motif (PAM). Expression of the dCas9-sMTase in mammalian cells led to predictable and efficient (up to ~70%) DNA methylation at targeted sites. Multiplexing sgRNAs enabled targeting methylation to multiple sites in a single promoter and to multiple sites in multiple promoters. This programmable de novo MTase tool might be used for studying mechanisms of initiation, spreading and inheritance of DNA methylation, and for therapeutic gene silencing.