Disease relevance of RIMS1

• Some of 'caps' was shown to be elongated normal lateral ventricle. 'Rims' of early stage revealed subependymal gliosis that was a part of normal aging processes [1].

High impact information on RIMS1

• In short-term plasticity, RIM1 accelerates the priming of synaptic vesicles for fusion; by contrast, in long-term potentiation of mossy fiber synapses in the hippocampal CA3 region, phosphorylated RIM1 acts through an unknown molecular pathway to enhance release of the excitatory neurotransmitter glutamate [2].
• Localization of a gene (CORD7) for a dominant cone-rod dystrophy to chromosome 6q [3].
• An analysis of the characteristics of the enhancement of secretion in permeabilized chromaffin cells indicates that N-terminal Rim1 does not alter the sensitivity of secretion to Ca(2+) but, instead, increases the rate of ATP-dependent priming of secretion [4].
• The zinc finger domain in Rim1 is unnecessary for Rab3a-GTP binding but, alone, enhances secretion [4].
• These findings demonstrate that hUCB, when transplanted into the spinal cord 7 days after weight-drop injury, survive for at least 2 weeks, differentiate into oligodendrocytes and neurons, and enable improved locomotor function [5].

Biological context of RIMS1

• Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7) [6].
• The RIM1 gene is composed of at least 35 exons, spans 577 kb of genomic DNA, and encodes a protein of up to 1693 residues [6].
• Given the genetic heterogeneity that features RP, it is plausible that mutations in RIM1 are also implicated in the disease in arRP families genetically linked to the CORD7 region [7].
• We have investigated the structural basis for the ability of Rim1 to bind Rab3a-GTP and to stimulate exocytosis in chromaffin cells [4].
• AIM: To characterise the phenotype of an autosomal dominant cone-rod dystrophy (CORD7) associated with the Arg844His mutation in RIM1 [8].

Anatomical context of RIMS1

• Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming [9].
• RIM1 is expressed in brain and photoreceptors of the retina where it is localised to the pre-synaptic ribbons in ribbon synapses [6].
• Rab3a binding and secretion-enhancing domains in Rim1 are separate and unique. Studies in adrenal chromaffin cells [4].
• In tracing group, Schwann cells (labeled with Hoechst) demonstrated their presence within spinal cord 7 days after transplantation [10].
• Maximum fraction-size equivalent dose values were: esophagus 5 Gy39; cord 7 Gy36 [11].

Associations of RIMS1 with chemical compounds

• RIM1, encoding a presynaptic protein involved in the glutamate neurotransmission, is the responsible gene for autosomal dominant cone-rod dystrophy CORD7, whose locus overlaps partially with a locus of autosomal recessive RP (arRP), RP25 [7].
• Like Rabphilin3, another putative Rab3a effector protein, Rim1 modulates secretion and contains a zinc-finger and two C2 domains [12].

Other interactions of RIMS1

• Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa [7].
• Labels of Bassoon, Piccolo and RIM 1, three active zone proteins, had very different distribution profiles from one another under control conditions [13].
• This locus appears to be distinct from, but adjacent to, the loci for cone-rod dystrophy 7 (CORD7) and North Carolina macular dystrophy (MCDR1) [14].

References