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Gene Review

RIMS1  -  regulating synaptic membrane exocytosis 1

Homo sapiens

Synonyms: CORD7, KIAA0340, Nbla00761, RAB3IP2, RIM, ...
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Disease relevance of RIMS1


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


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


  1. Pathologic findings of silent hyperintense white matter lesions on MRI. Takao, M., Koto, A., Tanahashi, N., Fukuuchi, Y., Takagi, M., Morinaga, S. J. Neurol. Sci. (1999) [Pubmed]
  2. RIM1: an edge for presynaptic plasticity. Lonart, G. Trends Neurosci. (2002) [Pubmed]
  3. Localization of a gene (CORD7) for a dominant cone-rod dystrophy to chromosome 6q. Kelsell, R.E., Gregory-Evans, K., Gregory-Evans, C.Y., Holder, G.E., Jay, M.R., Weber, B.H., Moore, A.T., Bird, A.C., Hunt, D.M. Am. J. Hum. Genet. (1998) [Pubmed]
  4. Rab3a binding and secretion-enhancing domains in Rim1 are separate and unique. Studies in adrenal chromaffin cells. Sun, L., Bittner, M.A., Holz, R.W. J. Biol. Chem. (2001) [Pubmed]
  5. Axonal remyelination by cord blood stem cells after spinal cord injury. Dasari, V.R., Spomar, D.G., Gondi, C.S., Sloffer, C.A., Saving, K.L., Gujrati, M., Rao, J.S., Dinh, D.H. J. Neurotrauma (2007) [Pubmed]
  6. Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7). Johnson, S., Halford, S., Morris, A.G., Patel, R.J., Wilkie, S.E., Hardcastle, A.J., Moore, A.T., Zhang, K., Hunt, D.M. Genomics (2003) [Pubmed]
  7. Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa. Barragan, I., Marcos, I., Borrego, S., Antiñolo, G. Ophthalmic Res. (2005) [Pubmed]
  8. A detailed study of the phenotype of an autosomal dominant cone-rod dystrophy (CORD7) associated with mutation in the gene for RIM1. Michaelides, M., Holder, G.E., Hunt, D.M., Fitzke, F.W., Bird, A.C., Moore, A.T. The British journal of ophthalmology. (2005) [Pubmed]
  9. Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming. Betz, A., Thakur, P., Junge, H.J., Ashery, U., Rhee, J.S., Scheuss, V., Rosenmund, C., Rettig, J., Brose, N. Neuron (2001) [Pubmed]
  10. Transplantation of Schwann cells to subarachnoid space induces repair in contused rat spinal cord. Firouzi, M., Moshayedi, P., Saberi, H., Mobasheri, H., Abolhassani, F., Jahanzad, I., Raza, M. Neurosci. Lett. (2006) [Pubmed]
  11. Feasibility report of image guided stereotactic body radiotherapy (IG-SBRT) with tomotherapy for early stage medically inoperable lung cancer using extreme hypofractionation. Hodge, W., Tomé, W.A., Jaradat, H.A., Orton, N.P., Khuntia, D., Traynor, A., Weigel, T., Mehta, M.P. Acta oncologica (Stockholm, Sweden) (2006) [Pubmed]
  12. Rim and exocytosis: Rab3a-binding and secretion-enhancing domains are separate and function independently. Sun, L., Bittner, M.A., Holz, R.W. Ann. N. Y. Acad. Sci. (2002) [Pubmed]
  13. Activity-related redistribution of presynaptic proteins at the active zone. Tao-Cheng, J.H. Neuroscience (2006) [Pubmed]
  14. A new locus for dominant drusen and macular degeneration maps to chromosome 6q14. Kniazeva, M., Traboulsi, E.I., Yu, Z., Stefko, S.T., Gorin, M.B., Shugart, Y.Y., O'Connell, J.R., Blaschak, C.J., Cutting, G., Han, M., Zhang, K. Am. J. Ophthalmol. (2000) [Pubmed]
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