Natali Chanaday
· Presidential Assistant ProfessorVerifiedUniversity of Pennsylvania · Physiology
Active 2009–2026
About
Natali Chanaday is a researcher whose work focuses on synaptic vesicle pools, their formation, organization, and maintenance, exploring the molecules, structure, and dynamics involved in these processes. Her research includes investigating the role of the endoplasmic reticulum in synaptic transmission, the regulation of neurotransmitter release, and the mechanisms of synaptic vesicle endocytosis. She has contributed to understanding how synaptic vesicles are recycled, the regulation of spontaneous and evoked neurotransmission, and the molecular interactions that govern synaptic function. Her work also encompasses studying the effects of various proteins such as synaptobrevin-2, VAMP4, and synaptotagmins on synaptic activity, as well as the impact of cellular stress and autoimmune conditions on neural communication. Chanaday's research has advanced knowledge of the modes and mechanisms of synaptic vesicle cycling, the role of calcium in these processes, and the presynaptic origins of neurotransmitter release, contributing significantly to the field of neurobiology.
Research topics
- Biology
- Neuroscience
- Chemistry
- Biochemistry
- Cell biology
Selected publications
Figshare · 2026-05-14
datasetOpen accessSupplementary Material 1
Figshare · 2026-05-14
articleOpen accessSupplementary Material 2
Figshare · 2026-05-14
articleOpen accessSupplementary Material 2
Journal of Nanobiotechnology · 2026-05-14
articleOpen accessSynaptic neurotransmission is a critical hallmark of brain activity and one of the first processes affected in neural diseases. Monitoring this process, particularly synaptic vesicle recycling, in living cells has been instrumental in revealing the mechanisms responsible for neurotransmitter release. However, currently available reporters suffer from limitations, such as large probe sizes or limited compatibility for human neurons, hampering the quantitative analysis of synaptic pathophysiology. Here, we describe the NbLumSyt1 toolkit, a panel of nanobody-based affinity probes that target the luminal domain of the synaptic vesicle protein Synaptotagmin 1 (Syt1). These new tools enable quantitative, noninvasive imaging and functional interrogation of Syt1 exo-endocytosis and trafficking in human neurons, with unprecedented precision, versatility and cost efficiency, in technologies ranging from fixed- and live-cell super-resolution imaging to electron microscopy and mass spectrometry. Overall, NbLumSyt1 nanobinders provide a valuable platform for studying synaptic physiology and pathophysiology, benefiting fundamental neuroscience and translational efforts to study and develop treatments for brain-related disorders.
Figshare · 2026-05-14
otherOpen accessAbstract Synaptic neurotransmission is a critical hallmark of brain activity and one of the first processes affected in neural diseases. Monitoring this process, particularly synaptic vesicle recycling, in living cells has been instrumental in revealing the mechanisms responsible for neurotransmitter release. However, currently available reporters suffer from limitations, such as large probe sizes or limited compatibility for human neurons, hampering the quantitative analysis of synaptic pathophysiology. Here, we describe the NbLumSyt1 toolkit, a panel of nanobody-based affinity probes that target the luminal domain of the synaptic vesicle protein Synaptotagmin 1 (Syt1). These new tools enable quantitative, noninvasive imaging and functional interrogation of Syt1 exo-endocytosis and trafficking in human neurons, with unprecedented precision, versatility and cost efficiency, in technologies ranging from fixed- and live-cell super-resolution imaging to electron microscopy and mass spectrometry. Overall, NbLumSyt1 nanobinders provide a valuable platform for studying synaptic physiology and pathophysiology, benefiting fundamental neuroscience and translational efforts to study and develop treatments for brain-related disorders. Graphical Abstract
Figshare · 2026-05-14
datasetOpen accessSupplementary Material 1
Figshare · 2026-05-14
otherOpen accessAbstract Synaptic neurotransmission is a critical hallmark of brain activity and one of the first processes affected in neural diseases. Monitoring this process, particularly synaptic vesicle recycling, in living cells has been instrumental in revealing the mechanisms responsible for neurotransmitter release. However, currently available reporters suffer from limitations, such as large probe sizes or limited compatibility for human neurons, hampering the quantitative analysis of synaptic pathophysiology. Here, we describe the NbLumSyt1 toolkit, a panel of nanobody-based affinity probes that target the luminal domain of the synaptic vesicle protein Synaptotagmin 1 (Syt1). These new tools enable quantitative, noninvasive imaging and functional interrogation of Syt1 exo-endocytosis and trafficking in human neurons, with unprecedented precision, versatility and cost efficiency, in technologies ranging from fixed- and live-cell super-resolution imaging to electron microscopy and mass spectrometry. Overall, NbLumSyt1 nanobinders provide a valuable platform for studying synaptic physiology and pathophysiology, benefiting fundamental neuroscience and translational efforts to study and develop treatments for brain-related disorders. Graphical Abstract
Pseudouridine selects RNAs for extracellular transport
bioRxiv (Cold Spring Harbor Laboratory) · 2025-10-30
preprintOpen accessRNAs move through the extracellular space to transmit information between cells, including mammalian neurons, yet how specific RNAs are channeled into these extracellular routes is unknown. Using genome-wide CRISPR screening, proteomics, and high-sensitivity transcriptomics in a neuronal cell line, we identify domesticated retroviral proteins and RNA-modifying enzymes that regulate RNA loading into and transportation via extracellular vesicles. We show that the pseudouridine synthase PUS1 is a key determinant of RNA trafficking, and that its catalytic product in RNA, pseudouridine, is both necessary and sufficient for extracellular RNA export. We further show that myosin light chain 6 (MYL6) is a pseudouridine-binding protein required for secretion of synthetic and endogenous RNAs. These findings reveal a biochemical code linking chemical RNA modification to extracellular transport, and establish a framework to study the function of extracellular RNAs in the nervous system and beyond.
bioRxiv (Cold Spring Harbor Laboratory) · 2025-04-20
preprintOpen accessAbstract Synaptic neurotransmission is a critical hallmark of brain activity and one of the first processes to be affected in neural diseases. Monitoring this process, and in particular synaptic vesicle recycling, in living cells has been instrumental in unraveling mechanisms responsible for neurotransmitter release. However, currently available reporters suffer from major limitations such large probe size or lack of suitability for human neurons, hampering the understanding of human synaptic pathophysiology. Here we describe the NbLumSyt1 toolkit, a panel of nanobody-based affinity probes targeting the luminal domain of the synaptic vesicle protein Synaptotagmin 1 (Syt1). These new tools enable quantitative, non-invasive imaging and functional interrogation of synaptic transmission in human neurons, with unprecedented precision, versatility and cost efficiency, in technologies ranging from fixed-and live-cell super-resolution imaging to electron microscopy and mass spectrometry. Overall, NbLumSyt1 nanobinders provide a valuable platform for human synaptic physiology and pathophysiology, benefiting fundamental neuroscience and translational efforts to study and develop treatments for brain-related disorders.
Astrocytes mobilize a broader repertoire of lysosomal repair mechanisms than neurons
bioRxiv (Cold Spring Harbor Laboratory) · 2025-09-08 · 1 citations
preprintOpen accessLysosomal damage impairs proteostasis and contributes to neurodegenerative diseases, yet cell-type-specific differences in lysosomal repair remain unclear. Using a neuron-astrocyte coculture system, we compared responses to lysosomal injury induced by a lysosomotropic methyl ester. Both neurons and astrocytes showed lysosomal damage, marked by galectin-3 recruitment to lumenal lysosomal β-galactosides, elevated lysosomal pH, and engagement of lysophagy receptors TAX1BP1 and p62. However, astrocytes showed a preferential recruitment of ESCRT repair machinery to damaged lysosomes. Additionally, the lysosomal membrane reformation pathway regulated by the RAB7-GAP, TBC1D15, was more robustly activated in astrocytes. By contrast, the PITT pathway, mediating lipid transfer between the ER and damaged lysosomes, was engaged in both cell types. Our data reveal a divergence in how neurons and astrocytes mobilize repair pathways to manage lysosomal damage. These data may reflect differences in lysosomal resilience between astrocytes and neurons and inform therapeutic strategies to correct lysosomal dysfunction in neurodegenerative diseases.
Frequent coauthors
- 31 shared
German A. Roth
Universidad Nacional de Córdoba
- 22 shared
Ege T. Kavalali
Vanderbilt University
- 16 shared
Nicolás Fernández Hurst
Consejo Nacional de Investigaciones Científicas y Técnicas
- 10 shared
Lisa M. Monteggia
Vanderbilt University
- 9 shared
Nicolás M. Díaz
Universidad de Los Andes
- 9 shared
Agustín Carbajal
Oklahoma Medical Research Foundation
- 9 shared
Guillermo G. Zampar
Research Centre in Biological Chemistry of Córdoba
- 9 shared
Carlos A. Arce
National University Toribio Rodríguez de Mendoza
Labs
Education
- 2008
Ph.D., Physiology
University of Pennsylvania
- 2002
B.S., Biology
University of California, San Diego
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