423 Medical Sciences Building
Office: (217) 244-6793
Lab: (217) 244-6749
Fax: (217) 244-1648
Mail to: Dept. of Cell and Developmental Biology
University of Illinois
601 S. Goodwin Avenue
Urbana, IL 61801
Associate Professor of Cell and Developmental Biology
Neurobiology, Protein-Nucleic Acid Interactions, Regulation of Gene Expression
Disease Research Interests
Neurological and Behavioral Disorders
B.S., University of Wisconsin-Madison (Bacteriology)
Ph.D., University of Wisconsin-Madison (Genetics)
Postdoctoral fellow, University of Chicago
Postdoctoral fellow, Emory University
Molecular basis of disease, post-translational modifications, regulation of RNA expression, RNA-protein interactions
The fragile X mental retardation protein FMRP is required for normal cognition: when it is absent, the most common form of inherited intellectual disability, fragile X syndrome (FXS) results. Thus, FMRP is a molecular entry point for understanding normal brain function. FMRP is an RNA binding protein that binds ~4% of brain mRNAs and regulates their expression—either enhancing or suppressing translation by an unknown mechanism. Bursts of protein translation are required for normal development and neuronal function but it is unknown how this process is regulated. We identified the RNA helicase MOV10 as a novel interactor of FMRP. MOV10 is elevated in developing brain and is required for viability as well as normal dendritic arborization and mouse behavior. Our goal is to understand how these RNA binding proteins function to facilitate learning and memory.
Kenny, P.J., Kim, M., Skariah, G., Nielsen, J., Lannom, M.C., and Ceman, S. 2020. The FMRP-MOV10 complex: A translational regulatory switch modulated by G-Quadruplexes. Nucleic Acids Research.
DeThorne, L. and Ceman, S. 2018. Genetic testing and autism: Tutorial for communication sciences and disorders. J. Communication Disorders. 74:61-73
Skariah, G., Perry, K. J., Drnevich, J., Henry, J. J. and Ceman, S. 2017. Mov10 is essential for gastrulation and CNS development. Dev Dyn. 247(4): 660-671. PMID:29266590 • Featured as the cover article 04/2018 • Referenced in a F1000 Faculty review
Skariah, G., Seimetz, J., Norsworthy, M., Lannom, M.C., Kenny, P. J., Elrakhawy, M., Forsthoefel, C., Drnevich, J., Kalsotra, A., Ceman. S. (2017). Mov10 suppresses retroelements and regulates neuronal development and function in developing brain. BMC Biology. 15(1):54 PMID:28662698 • Recommended by Faculty of 1000
Kenny, P. J. and Ceman, S. 2016. RNA secondary structure modulates FMRP’s bi-functional role in the microRNA pathway. International Journal of Molecular Sciences.17(6): pii: E985
Kenny, P.J., Zhou, H., Kim, M., Skariah, G., Khetani, R.S., Drnevich, J., Arcila, M.L., Kosik, K.S., Ceman, S. 2014. MOV10 and FMRP Regulate AGO2 Association with MicroRNA Recognition Elements. Cell Rep. 9(5): 1729-41
Kim, M. and S. Ceman. 2012. Fragile X Mental Retardation Protein: Past, Present and Future. Current Protein & Peptide Science. 13: 358-371
Blackwell, E. and Ceman, S. 2012. Arginine methylation of RNA binding proteins regulates cell function and differentiation. Molecular Reproductive Physiology.79:163-175
Winograd, C. and Ceman, S. 2011. Fragile X family members have important and non-overlapping functions. Biomolecular Concepts. Oct 1;2(5):343-52
Blackwell. E. and Ceman, S. 2011. Novel regulatory function of region proximal to RGG box in Fragile X Mental Retardation Protein. J. Cell Science. 124: 3060-3065.
Ceman, S. and Saugstad, J. 2011. MicroRNAs: Meta-controllers of gene expression in synaptic activity emerge as genetic and diagnostic markers of human disease. Pharmacology and Therapeutics. 130(1): 26-37.
Cheever, A., Blackwell, E., Ceman, S. 2010. Fragile X protein family member FXR1P is regulated by microRNAs. RNA.18 (8): 1530-1539
Blackwell, E. , Zhang, X. and Ceman, S. 2010. Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA. Hum. Mol. Gen.. 19(7): 1314-1323. PMC2838539.
Cheever, A. and Ceman. S. 2009. Phosphorylation of FMRP inhibits association with Dicer. RNA. 15(3): 362-366.