ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2001
An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
68 citing papers in PubMed, 169 citations in OpenAlex.
- A non-canonical ARMS-GABARAP interaction modulates dendritic spine formation and synaptic development.The EMBO journal · 2026Article
- Significantly higher rates of KIDINS220 polymorphisms in patients with obesity and end-stage renal disease.Obesity pillars · 2025Article
- Kidins220-deficient hydrocephalus mice exhibit altered glial phenotypes and AQP4 differential regulation in the retina and optic nerve, with preserved retinal ganglion cell survival.Fluids and barriers of the CNS · 2025Article
- Novel autosomal recessive SINO syndrome-associatedHeliyon · 2024Article
- Alterations in KIDINS220/ARMS Expression Impact Sensory Processing and Social Behavior in Adult Mice.International journal of molecular sciences · 2024Article
- Article
- Kidins220 sets the threshold for survival of neural stem cells and progenitors to sustain adult neurogenesis.Cell death & disease · 2023Article
- Mechanisms Controlling the Expression and Secretion of BDNF.Biomolecules · 2023Review
- ARMS-NF-κB signaling regulates intracellular ROS to induce autophagy-associated cell death upon oxidative stress.iScience · 2023Article
- Pre- and Postnatal Characterization of Autosomal RecessiveMolecular syndromology · 2022Article
- Transient Receptor Potential Vanilloid 1 Signaling Is Independent on Protein Kinase A Phosphorylation of Ankyrin-Rich Membrane Spanning Protein.Medical sciences (Basel, Switzerland) · 2022Article
- Article
- Phosphate dysregulation via the XPR1-KIDINS220 protein complex is a therapeutic vulnerability in ovarian cancer.Nature cancer · 2022Article
- Kidins220 deficiency causes ventriculomegaly via SNX27-retromer-dependent AQP4 degradation.Molecular psychiatry · 2021Article
- In vivo functions of p75Trends in pharmacological sciences · 2021Review
- Sorting nexin-27 regulates AMPA receptor trafficking through the synaptic adhesion protein LRFN2.eLife · 2021Article
- SINO Syndrome Causative KIDINS220/ARMS Gene Regulates Adipocyte Differentiation.Frontiers in cell and developmental biology · 2021Article
- Kidins220/ARMS controls astrocyte calcium signaling and neuron-astrocyte communication.Cell death and differentiation · 2020Article
- Differential regulation of Kidins220 isoforms in Huntington's disease.Brain pathology (Zurich, Switzerland) · 2020Article
- Excitotoxic targeting of Kidins220 to the Golgi apparatus precedes calpain cleavage of Rap1-activation complexes.Cell death & disease · 2019Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Appropriate development of nervous system connectivity involves a variety of processes, including neuronal life-and-death decisions, differentiation, axon guidance and migration, and synaptogenesis. Although these activities likely require specialized signaling events, few substrates unique to these neurotrophic functions have been identified. Here we describe the cloning of ankyrin repeat-rich membrane spanning (ARMS), which encodes a novel downstream target of neurotrophin and ephrin receptor tyrosine kinases, Trk and Eph, respectively. The amino acid sequence of ARMS is highly conserved from nematode to human, suggesting an evolutionarily conserved role for this protein. The ARMS protein consists of 1715 amino acids containing four putative transmembrane domains, multiple ankyrin repeats, a sterile alpha motif domain, and a potential PDZ-binding motif. In the rat, ARMS is specifically expressed in the developing nervous system and in highly plastic areas of the adult brain, regions enriched in Trks and Eph receptors. ARMS can physically associate with TrkA and p75 neurotrophin receptors. Moreover, endogenous ARMS protein is tyrosine phosphorylated after neurotrophin treatment of pheochromocytoma 12 cells and primary hippocampal neurons or ephrin B treatment of NG108-15 cells, demonstrating that ARMS is a downstream target for both neurotrophin and ephrin receptors.
Indexed as
Identifiers
11150334PMC6762419W1871356778What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.