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Mouse Anti-Rim Monoclonal Antibody, Unconjugated, Clone 26

RRID:AB_10611855

Antibody ID

AB_10611855

Target Antigen

Mouse Rim Clone 26 mouse, rat, rat, mouse

Proper Citation

(BD Biosciences Cat# 610907, RRID:AB_10611855)

Clonality

monoclonal antibody

Comments

vendor suggested use: IgG1 Western Blot, Immunofluorescence; Immunofluorescence; Western Blot

Host Organism

mouse

Vendor

BD Biosciences Go To Vendor

Cat Num

610907

Publications that use this research resource

RIM C2B Domains Target Presynaptic Active Zone Functions to PIP2-Containing Membranes.

  • de Jong APH
  • Neuron
  • 2018 Apr 18

Literature context:


Abstract:

Rapid and efficient synaptic vesicle fusion requires a pool of primed vesicles, the nearby tethering of Ca2+ channels, and the presence of the phospholipid PIP2 in the target membrane. Although the presynaptic active zone mediates the first two requirements, it is unclear how fusion is targeted to membranes with high PIP2 content. Here we find that the C2B domain of the active zone scaffold RIM is critical for action potential-triggered fusion. Remarkably, the known RIM functions in vesicle priming and Ca2+ influx do not require RIM C2B domains. Instead, biophysical experiments reveal that RIM C2 domains, which lack Ca2+ binding, specifically bind to PIP2. Mutational analyses establish that PIP2 binding to RIM C2B and its tethering to the other RIM domains are crucial for efficient exocytosis. We propose that RIM C2B domains are constitutive PIP2-binding modules that couple mechanisms for vesicle priming and Ca2+ channel tethering to PIP2-containing target membranes.

Funding information:
  • NCRR NIH HHS - S10 RR026461()
  • NIH HHS - S10 OD018027()
  • NIMH NIH HHS - R01 MH113349()
  • NINDS NIH HHS - P30 NS072030()
  • NINDS NIH HHS - R01 NS083898()
  • NINDS NIH HHS - R35 NS097333()
  • Wellcome Trust - GM043375(United Kingdom)

Dopamine Secretion Is Mediated by Sparse Active Zone-like Release Sites.

  • Liu C
  • Cell
  • 2018 Feb 8

Literature context:


Abstract:

Dopamine controls essential brain functions through volume transmission. Different from fast synaptic transmission, where neurotransmitter release and receptor activation are tightly coupled by an active zone, dopamine transmission is widespread and may not necessitate these organized release sites. Here, we determine whether striatal dopamine secretion employs specialized machinery for release. Using super resolution microscopy, we identified co-clustering of the active zone scaffolding proteins bassoon, RIM and ELKS in ∼30% of dopamine varicosities. Conditional RIM knockout disrupted this scaffold and, unexpectedly, abolished dopamine release, while ELKS knockout had no effect. Optogenetic experiments revealed that dopamine release was fast and had a high release probability, indicating the presence of protein scaffolds for coupling Ca2+ influx to vesicle fusion. Hence, dopamine secretion is mediated by sparse, mechanistically specialized active zone-like release sites. This architecture supports spatially and temporally precise coding for dopamine and provides molecular machinery for regulation.

Funding information:
  • NHLBI NIH HHS - R01 HL081398(United States)
  • NICHD NIH HHS - U54 HD090255()
  • NINDS NIH HHS - P30 NS072030()
  • NINDS NIH HHS - R01 NS083898()
  • NINDS NIH HHS - R01 NS103484()

Fusion Competent Synaptic Vesicles Persist upon Active Zone Disruption and Loss of Vesicle Docking.

  • Wang SSH
  • Neuron
  • 2016 Aug 17

Literature context:


Abstract:

In a nerve terminal, synaptic vesicle docking and release are restricted to an active zone. The active zone is a protein scaffold that is attached to the presynaptic plasma membrane and opposed to postsynaptic receptors. Here, we generated conditional knockout mice removing the active zone proteins RIM and ELKS, which additionally led to loss of Munc13, Bassoon, Piccolo, and RIM-BP, indicating disassembly of the active zone. We observed a near-complete lack of synaptic vesicle docking and a strong reduction in vesicular release probability and the speed of exocytosis, but total vesicle numbers, SNARE protein levels, and postsynaptic densities remained unaffected. Despite loss of the priming proteins Munc13 and RIM and of docked vesicles, a pool of releasable vesicles remained. Thus, the active zone is necessary for synaptic vesicle docking and to enhance release probability, but releasable vesicles can be localized distant from the presynaptic plasma membrane.

Funding information:
  • MRC - 200829/Z/16/Z(United Kingdom)

ELKS controls the pool of readily releasable vesicles at excitatory synapses through its N-terminal coiled-coil domains.

  • Held RG
  • Elife
  • 2016 Jun 2

Literature context:


Abstract:

In a presynaptic nerve terminal, synaptic strength is determined by the pool of readily releasable vesicles (RRP) and the probability of release (P) of each RRP vesicle. These parameters are controlled at the active zone and vary across synapses, but how such synapse specific control is achieved is not understood. ELKS proteins are enriched at vertebrate active zones and enhance P at inhibitory hippocampal synapses, but ELKS functions at excitatory synapses are not known. Studying conditional knockout mice for ELKS, we find that ELKS enhances the RRP at excitatory synapses without affecting P. Surprisingly, ELKS C-terminal sequences, which interact with RIM, are dispensable for RRP enhancement. Instead, the N-terminal ELKS coiled-coil domains that bind to Liprin-α and Bassoon are necessary to control RRP. Thus, ELKS removal has differential, synapse-specific effects on RRP and P, and our findings establish important roles for ELKS N-terminal domains in synaptic vesicle priming.