[HTML][HTML] Munc13-1 is a Ca2+-phospholipid-dependent vesicle priming hub that shapes synaptic short-term plasticity and enables sustained neurotransmission

N Lipstein, S Chang, KH Lin, FJ Lopez-Murcia, E Neher… - Neuron, 2021 - cell.com
During ongoing presynaptic action potential (AP) firing, transmitter release is limited by the
availability of release-ready synaptic vesicles (SVs). The rate of SV recruitment (SVR) to …

[HTML][HTML] The active-zone protein Munc13 controls the use-dependence of presynaptic voltage-gated calcium channels

N Calloway, G Gouzer, M Xue, TA Ryan - Elife, 2015 - elifesciences.org
Presynaptic calcium channel function is critical for converting electrical information into
chemical communication but the molecules in the active zone that sculpt this function are …

Nonconserved Ca2+/Calmodulin Binding Sites in Munc13s Differentially Control Synaptic Short-Term Plasticity

N Lipstein, S Schaks, K Dimova, S Kalkhof… - … and cellular biology, 2012 - Taylor & Francis
Munc13s are presynaptic proteins that mediate synaptic vesicle priming and thereby control
the size of the readily releasable pool of vesicles. During high synaptic activity, Munc13-1 …

[HTML][HTML] Heterodimerization of Munc13 C2A domain with RIM regulates synaptic vesicle docking and priming

M Camacho, J Basu, T Trimbuch, S Chang… - Nature …, 2017 - nature.com
The presynaptic active zone protein Munc13 is essential for neurotransmitter release,
playing key roles in vesicle docking and priming. Mechanistically, it is thought that the C2A …

[HTML][HTML] A C1-C2 module in Munc13 inhibits calcium-dependent neurotransmitter release

F Michelassi, H Liu, Z Hu, JS Dittman - Neuron, 2017 - cell.com
Almost all known forms of fast chemical synaptic transmission require the synaptic hub
protein Munc13. This essential protein has also been implicated in mediating several forms …

Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis

OH Shin, J Lu, JS Rhee, DR Tomchick… - Nature structural & …, 2010 - nature.com
Munc13 is a multidomain protein present in presynaptic active zones that mediates the
priming and plasticity of synaptic vesicle exocytosis, but the mechanisms involved remain …

[HTML][HTML] Characterization of the Munc13-calmodulin interaction by photoaffinity labeling

K Dimova, H Kawabe, A Betz, N Brose… - Biochimica et Biophysica …, 2006 - Elsevier
Sensing of and response to transient increases in the residual presynaptic Ca2+ levels are
important adaptive mechanisms that define the short-term plasticity characteristics of …

[HTML][HTML] Membrane bridging by Munc13-1 is crucial for neurotransmitter release

B Quade, M Camacho, X Zhao, M Orlando, T Trimbuch… - Elife, 2019 - elifesciences.org
Munc13-1 plays a crucial role in neurotransmitter release. We recently proposed that the C-
terminal region encompassing the C1, C2B, MUN and C2C domains of Munc13-1 …

Munc13-1 C1 domain activation lowers the energy barrier for synaptic vesicle fusion

J Basu, A Betz, N Brose… - Journal of Neuroscience, 2007 - Soc Neuroscience
Synapses need to encode a wide dynamic range of action potential frequencies. Essential
vesicle priming proteins of the Munc13 (mammalian Unc13) family play an important role in …

Tyrosine phosphorylation of Munc18‐1 inhibits synaptic transmission by preventing SNARE assembly

M Meijer, B Dörr, HCA Lammertse, C Blithikioti… - The EMBO …, 2018 - embopress.org
Tyrosine kinases are important regulators of synaptic strength. Here, we describe a key
component of the synaptic vesicle release machinery, Munc18‐1, as a phosphorylation …