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Senior Investigator

Mihaela Serpe, Ph.D.

Unit of Cellular Communication


Building 35 Room 1C-1016
Convent Drive
Bethesda 20892
Office: 301-443-3795


serpemih@mail.nih.gov

Dr. Mihaela (Ela) Serpe obtained her M.S. in Biochemistry from the University of Bucharest, Romania, then worked for two years in the Institute for Cellular Biology and Pathology “Nicolae Simionescu” in Bucharest. She completed a Ph.D. in Biochemistry at SUNY Buffalo in 1999 working with Dr. Dan Kosman on how yeast cells sense and acquire copper and iron from their environment. Driven by her interest in cellular signaling, she did postdoctoral training in the laboratory of Dr. Mike O’Connor at the University of Minnesota and Howard Hughes Medical Institute. Dr. Serpe started her own laboratory at NICHD in 2008. The long-term goal of her laboratory is to elucidate molecular mechanisms that regulate cell-cell communication during development. Her group is interested in two related key questions in cellular communication: (1) how are tissues patterned and correctly connected by short- and long-range signals, and (2) how are cells’ structures and functions coordinated at short range with those of their neighbors. Her lab investigates these processes using the Drosophila model system and focusing on early developmental patterning and the development of a specialized cell-cell interaction zone—the neuromuscular junction.



The purpose of the lab’s research is to elucidate molecular mechanisms that regulate cell-cell communication during development. The lab focuses on two related questions: 1) how are tissues patterned and correctly connected by long-range signals, and 2) how cells structures and functions are coordinated at short-range with those of their neighbors. BMPs modulate long-range signaling during patterning, but also ensure short-range communication at specialized cell-cell interaction zones, for example the neuromuscular junction (NMJ). Through studies on extracellular modulators of BMP signaling we aim to elucidate mechanisms that shape cell-cell communication during early patterning and at NMJ synapses.

In recent years, the lab has have initiated a groundbreaking project to understand the mechanisms of synapse assembly using the Drosophila NMJ as a genetic model. Drosophila NMJ is a glutamatergic synapse, similar in structure and physiology to mammalian central AMPA/Kainate synapses. In flies, each NMJ is unique and identifiable, synapses are large and accessible for electrophysiological and optical analysis, making the Drosophila NMJ a favorite genetic system to study synapse development. The subunits that form the glutamate-gated ion channels (iGluRs) are known and relatively well studied. However, the mechanisms that control iGluRs clustering and stabilization at postsynaptic densities remain a mystery. We have discovered a novel, essential protein, Neto (Neuropillin and Tolloid-like), that is absolutely required for iGluRs clustering at the Drosophila NMJ. Neto is the first auxiliary protein described in Drosophila and is the only non-channel subunit required for functional glutamate receptors. These findings provide an entry point to understand the molecular mechanisms of synapse development.

Interested in joining the lab? Visit the Openings page.
See where the lab was featured in the NIH Catalyst: https://irp.nih.gov/catalyst/v25i2/ambition-and-lots-of-fruit-flies.

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  • 1) Ramos CI, Igiesuorobo O, Wang Q, Serpe M. (2015)
  • Neto-mediated intracellular interactions shape postsynaptic composition at the Drosophila neuromuscular junction.
  • PLoS Genet., 11(4): e1005191.
  • 2) Han TH, Dharkar P, Mayer ML, Serpe M. (2015)
  • Functional reconstitution of Drosophila melanogaster NMJ glutamate receptors.
  • Proc Natl Acad Sci USA., 112(19): 6182-7.
  • 3) Sulkowski M, Kim YJ, Serpe M. (2014)
  • Postsynaptic glutamate receptors regulate local BMP signaling at the Drosophila neuromuscular junction.
  • Development., 141(2): 436-47.
  • 4) Kim YJ, Bao H, Bonanno L, Zhang B, Serpe M. (2012)
  • Drosophila Neto is essential for clustering glutamate receptors at the neuromuscular junction.
  • Genes Dev., 26(9): 974-87.
  • 5) Peluso CE, Umulis D, Kim YJ, O'Connor MB, Serpe M. (2011)
  • Shaping BMP morphogen gradients through enzyme-substrate interactions.
  • Dev Cell. , 21(2): 375-83.
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