Expertise
Research Summary
Our research focuses on the biogenesis, folding, and trafficking of acetylcholinesterase, the enzyme that terminates cholinergic neurotransmission in the central and peripheral nervous systems.
The vertebrate neuromuscular junction (NMJ) has long been used as a model for studying the development and function of synapses. My laboratory studies the biogenesis and regulation of acetylcholinesterase (AChE), the enzyme responsible for terminating neurotransmission at cholinergic synapses, as a marker for nerve-muscle interactions.
A second project involves the translational regulation of AChE by the RNA binding protein Pumilio2 that is highly localized to the NMJ. A third project involves the modulation of muscle AChE expression using specific peptides that can mimic portions of the non-catalytic subnits.
Dr. Rotundo is a cell biologist whose research focuses on acetylcholinesterase (AChE), an important component of the neuromuscular junction and all cholinergic synapses in the central and peripheral nervous systems
Our laboratory focuses on the regulation of neurotransmission via the enzyme, acetyl cholinesterase. We study: 1) The contributions of protein folding and assembly in regulating active molecules at synapses. 2) The development of novel probes for identifying cholinergic synapses. 3) RNA binding proteins that control protein translation at muscle and neuronal synapses in response to specific signals. 4) The repair of neuromuscular and CNS cholinergic synapse following acetylcholinesterase inactivation.
Keywords: Drug Discovery, Molecular Biology of RNA, DNA and Epigenetic Modifiers, Environmental Health and Toxicology