ArticleThe Journal of biological chemistry2012
Identification of NIPSNAP1 as a nocistatin-interacting protein involving pain transmission.
Article in The Journal of biological chemistry, 2012. 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, 25 citations in OpenAlex.
- Nipsnap1-A regulatory factor required for long-term maintenance of non-shivering thermogenesis.Molecular metabolism · 2023Article
- Knockdown of GBAS regulates esophageal cancer cell viability and apoptosis.Molecular medicine reports · 2021Article
- NIPSNAP protein family emerges as a sensor of mitochondrial health.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Review
- Systematic Discovery of Endogenous Human Ribonucleoprotein Complexes.Cell reports · 2019Article
- Endogenous Neuropeptide Nocistatin Is a Direct Agonist of Acid-Sensing Ion Channels (ASIC1, ASIC2 and ASIC3).Biomolecules · 2019Article
- Nocistatin sensitizes TRPA1 channels in peripheral sensory neurons.Channels (Austin, Tex.) · 2017Article
- Genetic and pharmacological evidence that endogenous nociceptin/orphanin FQ contributes to dopamine cell loss in Parkinson's disease.Neurobiology of disease · 2016Article
- Involvement of NIPSNAP1, a neuropeptide nocistatin-interacting protein, in inflammatory pain.Molecular pain · 2016Article
- KCMF1 (potassium channel modulatory factor 1) Links RAD6 to UBR4 (ubiquitin N-recognin domain-containing E3 ligase 4) and lysosome-mediated degradation.Molecular & cellular proteomics : MCP · 2015Article
- Functional plasticity of the N/OFQ-NOP receptor system determines analgesic properties of NOP receptor agonists.British journal of pharmacology · 2014Review
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Authors and funding
8 authors at 7 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
4-Nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1 (NIPSNAP1) is a molecule of physiologically unknown function, although it is predominantly expressed in the brain, spinal cord, liver, and kidney. We identified NIPSNAP1 as a protein that interacts with the neuropeptide nocistatin (NST) from synaptosomal membranes of mouse spinal cord using high-performance affinity latex beads. NST, which is produced from the same precursor protein as an opioid-like neuropeptide nociceptin/orphanin FQ (N/OFQ), has opposite effects on pain transmission evoked by N/OFQ. The calculated full-length pre-protein of NIPSNAP1 was 33 kDa, whereas the N-terminal truncated form of NIPSNAP1 (29 kDa) was ubiquitously expressed in the neuronal tissues, especially in synaptic membrane and mitochondria of brain. The 29-kDa NIPSNAP1 was distributed on the cell surface, and NST interacted with the 29-kDa but not the 33-kDa NIPSNAP1. Although intrathecal injection of N/OFQ induced tactile allodynia in both wild-type and NIPSNAP1-deficient mice, the inhibition of N/OFQ-evoked tactile allodynia by NST seen in wild-type mice was completely lacking in the deficient mice. These results suggest that NIPSNAP1 is an interacting molecule of NST and plays a crucial role in pain transmission.
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