Skip to Main Content

Elizabeth Jonas, MD

Harvey and Kate Cushing Professor of Medicine (Endocrinology) and Professor of Neuroscience
DownloadHi-Res Photo

About

Titles

Harvey and Kate Cushing Professor of Medicine (Endocrinology) and Professor of Neuroscience

Biography

Elizabeth Jonas received training in Neurology and Internal Medicine. She developed an interest in Neuroscience while studying as a medical student with Dr. Rodolfo Llinas at N.Y.U. and at the Marine Biological Laboratory. With Dr. Llinas she developed an interest in calcium control of synaptic transmission. She pursued this interest as a post-doctoral fellow in the laboratory of Dr. Leonard Kaczmarek, Yale Pharmacology. Dr. Jonas developed a technique for recording from ion channels on intracellular membranes and has used this and other techniques to study mitochondria. Mitochondria are necessary for life and death of neurons and other cells. Regulation of mitochondrial metabolism is also key to energy efficiency in the nervous system. Dr. Jonas is now studying the role of mitochondria and energy efficiency in neurodegenerative disease states and in learning and memory formation in healthy brain. Her lab has recently characterized the molecular identity of the cell death channel known as the mitochondrial permeability transition pore and is now studying how inhibiting gating of the pore may ameliorate stroke, neurodegenerative and developmental brain diseases.

Appointments

Education & Training

MD
New York University (1986)
BA
Yale University (1982)

Board Certifications

  • Neurology

    Certification Organization
    AB of Psychiatry & Neurology
    Original Certification Date
    1991

Research

Overview

  • Role of ATP synthase in prevention of cardiac and brain ischemia: Mitochondrial ATP synthase has been shown recently to be vital not only for cellular energy production but also for energy dissipation and cell death. We identified and characterized a large non-selective uncoupling channel within the ATP synthase c-subunit ring, the persistent opening of which initiates cell death. We have growing evidence for its crucial role in mitochondrial permeability transition (mPT), the opening of a cell death channel that regulates neuronal death during ischemia and neurodegeneration. We have found that the c-ring channel is also required for certain critical periods in brain development, and that normal closing of the channel is required for normal brain and synaptic development. We have now purified ATP synthase from porcine heart mitochondria and performed single-channel studies.
  • Structural studies of the ATP synthase c-ring pore: Excised proteoliposome patch-clamp recordings demonstrate that highly pure and fully assembled ATP synthase monomers form large conductance, Ca2+-sensitive and voltage-gated channels. We have confirmed the monomeric state of ATP synthase by cryo-electron microscopy studies of ATP synthase reconstituted into proteoliposomes. We have also heterologously overexpressed and purified human ATP synthase c-subunit fromHEK-293 cells and from E. coli plasma membranes. C-subunit ring purified using this technique forms large conductance channels. C-ring channel is gated by polar amino acid residues situated at the mouth of the pore and by the hydrophilic F1 portion of ATP synthase. We observe dissociation of ATP synthase F1 from FO when we expose primary neurons to glutamate toxicity, suggesting that the non-reversible dissociation of F1 from FO occurs in pathology. We have successfully knocked out five/six alleles of the three genes encoding ATP synthase c-subunit in mouse embryonic stem cells by CRISPR-Cas9, which resulted in 10 percent of the total c-subunit expression. Patch-clamp recordings of mitoplasts isolated from these cells demonstrate low conductance activity that is poorly calcium responsive. These findings confirm that the largest of all inner mitochondrial membrane conductances, and one that forms an uncoupling, non-selective leak channel, resides within the ATP synthase monomer, more specifically within its membrane-embedded c-subunit ring. We are now creating a mouse with a mutant c-subunit that contains a reduced conductance c-subunit. We hypothesize that this mouse will be protected from ischemic heart and brain disease and from degenerative diseases.
  • Role of mitochondria in Fragile X disorder: Loss of function of the gene (Fmr1) encoding Fragile X mental retardation protein (FMRP) results in unregulated, elevated mRNA translation and aberrant synaptic morphology. We find that mitochondria in neurons of the Fmr1-/y mouse have an inner membrane leak that undermines ATP synthesis and contributes to a replicative phenotype that is a hallmark of immature, dividing cells. We now find that abnormal stoichiometry leading to increased free ATP synthase c-subunit ring contributes to aberrant mRNA translation in Fmr1-/y mouse neurons and human Fragile X Syndrome (FXS) fibroblasts. C-subunit leak inhibition alters metabolism in favor of oxidative phosphorylation, ushering in a new synaptic developmental period, and this critical change fails to occur in Fragile X synapses. The developmental metabolic switch is also dependent on stimulus-induced phosphorylation of translation elongation factor EF2, an event which is lacking in Fmr1-/y synapses and which changes the mRNAs that are translated. We find that FMRP regulates a stimulus-dependent change in mitochondrial metabolism required for synaptic development.
  • Role of Bcl-xL in synaptic plasticity: Long-term potentiation (LTP) and depression (LTD) are the mechanisms that neurons use to modulate their inherent synaptic plasticity and support the storage and recovery of memories in the mammalian brain. The ability to potentiate a synapse over the long term declines significantly in neurodegenerative disorders. In addition to deficiencies in synaptic plasticity, degenerating neurons display acute and chronic mitochondrial dysfunction, suggesting that dysregulated mitochondria play a role in synaptic dysfunction, in addition to their known role in apoptotic cell death. Our previous work has shown that the anti-apoptotic protein Bcl-xL not only prevents somatic cell death, but also potentiates long-term synaptic responses. Here, we show that Bcl-xL is responsible for dramatic changes in ATP levels in hippocampal neurons during LTP. Using fluorescence imaging of a FRET based ATP construct (ATeam) in living hippocampal neurons, we find that LTP induction causes a sharp decrease in ATP levels followed by a persistent long term increase in ATP production. This suggests that after intense synaptic stimulation, neurons may become metabolically more efficient. The long-term increase in ATP levels of LTP-stimulated synapses is blocked by inhibition of Bcl-xL and by inhibition of ATP synthase activity. Bcl-xL inhibition also prevents the long-term increase in surface glutamate receptor insertion. In hippocampal slice recordings, inhibition of Bcl-xL impairs early stage LTP and prevents late stage LTP. Our findings suggest that long term changes in mitochondrial efficiency brought on by activity-dependent translocation of Bcl-xL to mitochondria are required for LTP and shed light upon the role of mitochondrial metabolic programming and dynamics in acute induction and long-term maintenance of learning and memory processing. If such mitochondria-dependent metabolic changes fail to occur, synaptic dysfunction and neurodegeneration may ensue.
  • Role of mitochondrial bioenergetics in Parkinson's Disease: Familial Parkinson’s disease (PD) protein DJ-1 mutations are linked to early onset PD. We have found that DJ-1 binds directly to the F1FO ATP synthase β subunit to increase the enzymatic activity of the ATP synthase and enhance the efficiency of ATP production. Mutations in DJ-1 or DJ-1 knock out cause loss of mitochondrial inner membrane coupling, resulting in decreased growth of mouse dopaminergic neuronal processes and human fibroblasts. the reason for this is loss of DJ-1 decreases ATP synthase β subunit levels. DJ-1 improves ATP synthase β subunit levels by boosting its translation and by chaperoning β subunit into the mitochondria. We suggest that DJ-1 maximizes inner membrane efficiency by improving F1/FO ratio. This decreases the inner mitochondrial membrane leak, enhancing dopaminergic neuronal process extension.



Medical Subject Headings (MeSH)

Apoptosis; Endocrinology; Mitochondria; Nervous System; Neurobiology; Synaptic Transmission

Research at a Glance

Yale Co-Authors

Frequent collaborators of Elizabeth Jonas's published research.

Publications

2024

2023

2022

Academic Achievements & Community Involvement

  • honor

    Elected Member

  • activity

    Mitochondria and Synaptic Plasticity: Role of ATP synthase in synaptic function and neuronal degeneration

Get In Touch