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Human Polyclonal RIMS1 Primary Antibody pour ICC, IHC - ABIN1742305
Bello, Zanetti, Mayorga, Michaut: RIM, Munc13, and Rab3A interplay in acrosomal exocytosis. dans Experimental cell research 2012
Show all 11 Pubmed References
Rat (Rattus) Polyclonal RIMS1 Primary Antibody pour ICC, IHC - ABIN1742306
Limbach, Laue, Wang, Hu, Thiede, Hultqvist, Kilimann: Molecular in situ topology of Aczonin/Piccolo and associated proteins at the mammalian neurotransmitter release site. dans Proceedings of the National Academy of Sciences of the United States of America 2011
Postsynaptic RIM1 in hippocampal CA1 region is required for basal NMDAR-, but not AMPA receptor (AMPAR)-, mediated synaptic responses, and contributes to synaptic plasticity and hippocampus-dependent memory. Moreover, RIM1 levels in hippocampal neurons influence both the constitutive and regulated NMDAR trafficking, without affecting constitutive AMPAR trafficking.
Here, the authors show that exophilin-8 accumulates granules in the cortical F-actin network not by direct interaction with myosin-Va, but by indirect interaction with a specific form of myosin-VIIa through its previously unknown binding partner, RIM-BP2.
RBPs perform unexpectedly broad roles at the active zone that together with those of RIMs are essential for all active zone functions.
Electrophysiological characterization of VDCC currents revealed that the suppressive effect of RIM2alpha on voltage-dependent inactivation (VDI) was stronger than that of RIM1alpha for the CaV2.1 variant containing the region encoded by exons 44 and 47.
The function of RIM1/2 at rod ribbons is to enhance Cav1.4 channel activity, possibly through direct or indirect modulation of the channel.
Experiments with single Rim 1/2 gene inactivation at the large calyx of Held synapse show largely overlapping roles of the two major Rim genes in vesicle priming/docking
RIM1alpha can influence short-term plasticity at cerebellar parallel-fibre synapses.
betaARs couple to a cAMP/Epac/PLC/Munc13-1/Rab3a/RIM1a-dependent pathway to enhance glutamate release at cerebrocortical nerve terminals.
RIM1alpha has a role in synaptic vesicle tethering.
Presynaptic plasticity and function of RIM1a play an important part in the neuron's adaptive response to aberrant electrical activity following pharmacologically induced status epielepticus.
The interaction between RIM1alpha and Munc13-1 is required for presynaptic long-term plasticity
Data suggest that RIM1/2 proteins co-ordinately regulate key functions for fast transmitter release, enabling a high presynaptic Ca(2)+ channel density and vesicle docking at the active zone.
In addition to RIM1alpha's involvement in multiple behavioral abnormalities, these data suggest that alterations in presynaptic forms of short-term plasticity are linked to alterations in prepulse inhibition, a measure of sensorimotor gating.
RIM1alpha interacts with several active zone molecules, including Munc13-1 and alpha-liprins, to form a protein scaffold in the presynaptic nerve terminal.
required for presynaptic long-term potentiation.
Results suggest that protein kinase A-mediated phosphorylation of the active zone protein RIM1alpha at a single N-terminal site induces presynaptic long-term potentiation.
Mice with a synaptotagmin 1 mutation, which lowers release probability, and mice with Rab3A deletion, which abolishes presynaptic long-term potentiation, the combination of presynaptic abnormalities in RIM1alpha mice severely alters learning and memory.
Rab3A-interacting molecule RIM regulates the presynaptic recruitment of Munc13-1 and ubMunc13-2
These data demonstrate that alpha-RIMs are not essential for synapse formation or synaptic exocytosis, but are required for normal Ca(2+)-triggering of exocytosis.
A possible role for RIMS1 in the enhancement of cognitive function at least in this kindred is suggested.
This is the first reported case of bilateral cystoid macular edema in association with the RIM1 mutation. Overall, our findings were more consistent with a phenotype of retinitis pigmentosa.
The study identified a region on chromosome 6 comprising the genes SMAP1, B3GAT2, and RIMS1 as novel susceptibility locus for pediatric venous thromboembolism.
Here, we report that, like Rab3A, RIM and Munc13 are present in human sperm and that they play a functional role in acrosomal exocytosis before the acrosomal calcium efflux
a novel functional coupling between RIM1 and the L-type Ca(V) channels via the Ca(V)beta auxiliary subunit that contribute to determine insulin secretion.
Rim1 modulates direct G-protein regulation of Ca(v)2.2 channels.
Rim1 is a component of the presynaptic active zone and modulator of exocytosis and binds 14-3-3 through its N terminus
Even though the absence of pathogenic mutations suggests that RIM1 is notinvolved in autosomal recessive retinitis pigmentosa.
The protein encoded by this gene is a RAS gene superfamily member that regulates synaptic vesicle exocytosis. This gene also plays a role in the regulation of voltage-gated calcium channels during neurotransmitter and insulin release. Mutations have suggested a role cognition and have been identified as the cause of cone-rod dystrophy type 7. Multiple transcript variants encoding different isoforms have been described for this gene.
regulating synaptic membrane exocytosis 1
, regulating synaptic membrane exocytosis protein 1-like
, regulating synaptic membrane exocytosis protein 1
, RIM 1
, Rab3 effector
, Rab3 interacting protein 1
, rab-3-interacting molecule 1
, rab-3-interacting protein 1
, rab3-interacting molecule 1
, rab3-interacting protein 1
, synaptic exocytosis regulator 1
, RAB3-interacting protein 2
, rab-3-interacting protein 2
, Rim1b protein