ArticleBiochimica et biophysica acta2013
Direct association of the reticulon protein RTN1A with the ryanodine receptor 2 in neurons.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Inter-Organelle Membrane Contact Sites as Physiological Regulatory Hubs in the Brain: From Neurons to Glial Cells.Biomolecules · 2026Review
- Reticulon-1 synthesis controls outgrowth and microtubule dynamics in injured cortical axons.Life science alliance · 2026Article
- Genetic admixture and adaptive signatures of Guanling cattle revealed by whole-genome sequence.BMC genomics · 2026Article
- Interoperability of RTN1A in dendrite dynamics and immune functions in human Langerhans cells.eLife · 2022Article
- Distinct Distribution of RTN1A in Immune Cells in Mouse Skin and Lymphoid Organs.Frontiers in cell and developmental biology · 2020Article
- Specific Proteomes of Hippocampal Regions CA2 and CA1 Reveal Proteins Linked to the Unique Physiology of Area CA2.Journal of proteome research · 2019Article
- Human Olfactory Ensheathing Cell Transplantation Improves Motor Function in a Mouse Model of Type 3 Spinocerebellar Ataxia.Cell transplantation · 2017Article
- RTN1 and RTN3 protein are differentially associated with senile plaques in Alzheimer's brains.Scientific reports · 2017Article
- The role of reticulons in neurodegenerative diseases.Neuromolecular medicine · 2014Review
- Nogo-A couples with Apg-1 through interaction and co-ordinate expression under hypoxic and oxidative stress.The Biochemical journal · 2013Article
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Authors and funding
12 authors.
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Abstract
RTN1A is a reticulon protein with predominant localization in the endoplasmic reticulum (ER). It was previously shown that RTN1A is expressed in neurons of the mammalian central nervous system but functional information remains sparse. To elucidate the neuronal function of RTN1A, we chose to focus our investigation on identifying possible novel binding partners specifically interacting with the unique N-terminus of RTN1A. Using a nonbiased approach involving GST pull-downs and MS analysis, we identified the intracellular calcium release channel ryanodine receptor 2 (RyR2) as a direct binding partner of RTN1A. The RyR2 binding site was localized to a highly conserved 150-amino acid residue region. RTN1A displays high preference for RyR2 binding in vitro and in vivo and both proteins colocalize in hippocampal neurons and Purkinje cells. Moreover, we demonstrate the precise subcellular localization of RTN1A in Purkinje cells and show that RTN1A inhibits RyR channels in [(3)H]ryanodine binding studies on brain synaptosomes. In a functional assay, RTN1A significantly reduced RyR2-mediated Ca(2+) oscillations. Thus, RTN1A and RyR2 might act as functional partners in the regulation of cytosolic Ca(2+) dynamics the in neurons.
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