Synaptic mitochondria as critical organelles in the process of synaptic transmission, a highly energy dependent process requiring large amounts of localized adenosine triphosphate (ATP). In addition to generating ATP to meet energetic demands, synaptic mitochondria are also important for calcium homeostasis, regulation of reactive oxygen species, and neuronal plasticity. In proteopathic neurodegenerative conditions such as Alzheimer's (AD) or Parkinson's disease (PD) aberrant protein homeostasis including accumulation of toxic protein species coincides with impaired mitochondrial function, neurotransmitter release, and altered redox balance. Importantly, these features of neurodegeneration precede synaptic failure and neuronal death.
While synaptic failure, mitochondrial dysfunction, and pathological protein accumulation are common features of many neurodegenerative disorders, the pathology and specific toxic protein (e.g., tau in AD and alpha-synuclein in PD) of these diseases are diverse. Correlative research suggests that a common link exists between these features and a great investigative effort has been made thus far to determine this link mechanistically. In vitro work has begun to yield small pieces of the puzzle, however, in vivo results are less consistent. Therefore, a need exists to better characterize the overlap while identifying key differences that contribute to the observed pathological differences between neurodegenerative disorders.
This Research Topic aims to bring together high-quality manuscripts in the form of Original Research Articles, Reviews, and Brief Research Reports that focus on uncovering or summarizing mechanistic links between the common proteopathic protein accumulation, synaptic bioenergetics, and synaptic failure that precede neurodegeneration. Within that scope, we welcome original research article submissions from diverse fields and disciplines with a special interest given to those that emphasize structural and biophysical characterization of proteopathic species in correlation with their impact on synaptic bioenergetics or function. Due to the ambiguous nature of the physiological functions of proteopathic proteins, we also welcome investigations that seek to better characterize the physiological roles these proteins play and early events that lead to the initiation of their pathological effects.
The Research Topic Coordinator, Dr. Andrew J. Trease, is currently a senior post-doctoral research associate at the University of Nebraska Medical Center in the Department of Neurological Sciences. His primary current research focus is understanding the biochemical and biophysical properties that underlie the pathological effects of tau accumulation in the context of Alzheimer's disease and related dementias, and how this affects mitochondrial function in the synapse.
Keywords:
mitochondria, protein-protein interaction, tau, oligomer, neurodegeneration, Alzheimer's, Parkinson's, Huntingtons, proteostasis, bioenergetics
Important Note:
All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.
Synaptic mitochondria as critical organelles in the process of synaptic transmission, a highly energy dependent process requiring large amounts of localized adenosine triphosphate (ATP). In addition to generating ATP to meet energetic demands, synaptic mitochondria are also important for calcium homeostasis, regulation of reactive oxygen species, and neuronal plasticity. In proteopathic neurodegenerative conditions such as Alzheimer's (AD) or Parkinson's disease (PD) aberrant protein homeostasis including accumulation of toxic protein species coincides with impaired mitochondrial function, neurotransmitter release, and altered redox balance. Importantly, these features of neurodegeneration precede synaptic failure and neuronal death.
While synaptic failure, mitochondrial dysfunction, and pathological protein accumulation are common features of many neurodegenerative disorders, the pathology and specific toxic protein (e.g., tau in AD and alpha-synuclein in PD) of these diseases are diverse. Correlative research suggests that a common link exists between these features and a great investigative effort has been made thus far to determine this link mechanistically. In vitro work has begun to yield small pieces of the puzzle, however, in vivo results are less consistent. Therefore, a need exists to better characterize the overlap while identifying key differences that contribute to the observed pathological differences between neurodegenerative disorders.
This Research Topic aims to bring together high-quality manuscripts in the form of Original Research Articles, Reviews, and Brief Research Reports that focus on uncovering or summarizing mechanistic links between the common proteopathic protein accumulation, synaptic bioenergetics, and synaptic failure that precede neurodegeneration. Within that scope, we welcome original research article submissions from diverse fields and disciplines with a special interest given to those that emphasize structural and biophysical characterization of proteopathic species in correlation with their impact on synaptic bioenergetics or function. Due to the ambiguous nature of the physiological functions of proteopathic proteins, we also welcome investigations that seek to better characterize the physiological roles these proteins play and early events that lead to the initiation of their pathological effects.
The Research Topic Coordinator, Dr. Andrew J. Trease, is currently a senior post-doctoral research associate at the University of Nebraska Medical Center in the Department of Neurological Sciences. His primary current research focus is understanding the biochemical and biophysical properties that underlie the pathological effects of tau accumulation in the context of Alzheimer's disease and related dementias, and how this affects mitochondrial function in the synapse.
Keywords:
mitochondria, protein-protein interaction, tau, oligomer, neurodegeneration, Alzheimer's, Parkinson's, Huntingtons, proteostasis, bioenergetics
Important Note:
All contributions to this Research Topic must be within the scope of the section and journal to which they are submitted, as defined in their mission statements. Frontiers reserves the right to guide an out-of-scope manuscript to a more suitable section or journal at any stage of peer review.