Topographical distance between presynaptic Ca 2+ channels and exocytotic Ca 2+ sensors contributes to differential facilitatory actions of roscovitine on neurotransmitter release at cerebellar glutamatergic and GABAergic synapses

2021 ◽  
Author(s):  
Shin’Ichiro Satake ◽  
Shiro Konishi
Keyword(s):  
Neurotransmitter Release ◽  
Gabaergic Synapses

RIM function in short- and long-term synaptic plasticity

2005 ◽  
Vol 33 (6) ◽  
pp. 1345-1349 ◽  
Author(s):  
P.S. Kaeser ◽  
T.C. Südhof
Keyword(s):  
Synaptic Plasticity ◽  
Active Zone ◽  
Neurotransmitter Release ◽  
Mossy Fibre ◽  
Short Term ◽  
Parallel Fibre ◽  
Ca1 Region ◽  
Gabaergic Synapses ◽  
Protein Rich

RIM1α (Rab3-interacting molecule 1α) is a large multidomain protein that is localized to presynaptic active zones [Wang, Okamoto, Schmitz, Hofmann and Südhof (1997) Nature (London) 388, 593–598] and is the founding member of the RIM protein family that also includes RIM2α, 2β, 2γ, 3γ and 4γ [Wang and Südhof (2003) Genomics 81, 126–137]. In presynaptic nerve termini, RIM1α interacts with a series of presynaptic proteins, including the synaptic vesicle GTPase Rab3 and the active zone proteins Munc13, liprins and ELKS (a protein rich in glutamate, leucine, lysine and serine). Mouse KOs (knockouts) revealed that, in different types of synapses, RIM1α is essential for different forms of synaptic plasticity. In CA1-region Schaffer-collateral excitatory synapses and in GABAergic synapses (where GABA is γ-aminobutyric acid), RIM1α is required for maintaining normal neurotransmitter release and short-term synaptic plasticity. In contrast, in excitatory CA3-region mossy fibre synapses and cerebellar parallel fibre synapses, RIM1α is necessary for presynaptic long-term, but not short-term, synaptic plasticity. In these synapses, the function of RIM1α in presynaptic long-term plasticity depends, at least in part, on phosphorylation of RIM1α at a single site, suggesting that RIM1α constitutes a ‘phosphoswitch’ that determines synaptic strength. However, in spite of the progress in understanding RIM1α function, the mechanisms by which RIM1α acts remain unknown. For example, how does phosphorylation regulate RIM1α, what is the relationship of the function of RIM1α in basic release to synaptic plasticity and what is the physiological significance of different forms of RIM-dependent plasticity? Moreover, the roles of other RIM isoforms are unclear. Addressing these important questions will contribute to our view of how neurotransmitter release is regulated at the presynaptic active zone.

Molecular analysis of neurotransmitter release

1998 ◽  
Vol 33 ◽  
pp. 29-41 ◽  
Author(s):  
Giampietro Schiavo ◽  
Gudrun Stenbeck
Keyword(s):  
Molecular Analysis ◽  
Neurotransmitter Release
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