Josep Rizo is a Professor of Biophysics, Biochemistry and Pharmacology at the University of Texas Southwestern Medical Center, where he is Virginia Lazenby O'Hara Chair in Biochemistry. He is particularly interested in the study of the mechanisms of neurotransmitter release and intracellular membrane fusion using structural biology, a variety of biophysical techniques and reconstitution approaches. Jose has been a part of the FEBS Open Bio Editorial Board since 2021. In this interview, he shares his insights into developments in the field of neurotransmitter release, describes his move from Spain to the United States, and discusses how sometimes you need to use both logic and scientific hunches.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10761924 | PMC |
| http://dx.doi.org/10.1002/2211-5463.13746 | DOI Listing |
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Neurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface.
Proc Natl Acad Sci U S A
October 2024
Institute of Neurophysiology, Charité-Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin 10117, Germany.
The Ca sensor synaptotagmin-1 (Syt1) triggers neurotransmitter release together with the neuronal sensitive factor attachment protein receptor (SNARE) complex formed by syntaxin-1, SNAP25, and synaptobrevin. Moreover, Syt1 increases synaptic vesicle (SV) priming and impairs spontaneous vesicle release. The Syt1 CB domain binds to the SNARE complex through a primary interface via two regions (I and II), but how exactly this interface mediates distinct functions of Syt1 and the mechanism underlying Ca triggering of release are unknown.
View Article and Find Full Text PDFNeurotransmitter release is triggered by a calcium-induced rearrangement in the Synaptotagmin-1/SNARE complex primary interface.
bioRxiv
June 2024
Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Neurophysiology, Berlin, Germany.
The Ca sensor synaptotagmin-1 triggers neurotransmitter release together with the neuronal SNARE complex formed by syntaxin-1, SNAP25 and synaptobrevin. Moreover, synaptotagmin-1 increases synaptic vesicle priming and impairs spontaneous vesicle release. The synaptotagmin-1 CB domain binds to the SNARE complex through a primary interface via two regions (I and II), but how exactly this interface mediates distinct functions of synaptotagmin-1, and the mechanism underlying Ca-triggering of release is unknown.
View Article and Find Full Text PDFA lever hypothesis for Synaptotagmin-1 action in neurotransmitter release.
bioRxiv
June 2024
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
Article Synopsis
- Neurotransmitter release happens quickly through the interaction of calcium (Ca) with Synaptotagmin-1 and the formation of SNARE complexes, but how these interactions lead to membrane fusion is still unclear.
- Synaptotagmin-1's Ca-binding loops were thought to help merge membranes, but new simulations show they might actually hinder SNARE function, contradicting older models.
- Recent experiments suggest that when Ca binds to Synaptotagmin-1, it reorients the protein in a way that aids in bringing SNARE complexes together for membrane fusion, acting like a lever to enhance the process.
Molecular mechanism underlying SNARE-mediated membrane fusion enlightened by all-atom molecular dynamics simulations.
Proc Natl Acad Sci U S A
April 2024
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390.
Article Synopsis
- SNARE proteins (syntaxin-1, SNAP-25, synaptobrevin) play a crucial role in rapidly releasing neurotransmitters by forming complexes that fuse synaptic vesicles with cell membranes within microseconds.* -
- Current theories suggest that these proteins work mechanically like rods, zipping together to bring membranes closer, but the exact mechanism of fast fusion is still unclear.* -
- Molecular dynamics simulations propose a new model where the zippering of SNARE helices initiates fusion at a local level, expanding hydrophobic regions to form fusion pores, and indicates that polyunsaturated lipids might enhance the efficiency of this process.*
Control of Munc13-1 Activity by Autoinhibitory Interactions Involving the Variable N-terminal Region.
J Mol Biol
April 2024
Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address:
Article Synopsis
- Regulation of neurotransmitter release is crucial for different types of information processing in the brain, with Munc13 proteins being key players in this process.
- Munc13-1 has specific domains, including a calmodulin binding (CaMb) domain for short-term plasticity and a CA domain that dimerizes and interacts with other proteins influencing presynaptic activity.
- Research indicates that the Munc13-1's activity is inhibited by interactions between its domains but can be enhanced by other proteins like RIM2α and calmodulin, highlighting a complex mechanism of regulating neurotransmitter release.
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