ArticleThe Journal of biological chemistry2014
Amigo adhesion protein regulates development of neural circuits in zebrafish brain.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Multimodal AI fuses proteomic and EHR data for rational prioritization of protein biomarkers in diabetic retinopathy.medRxiv : the preprint server for health sciences · 2026Article
- PCM1 coordinates centrosome asymmetry with polarized endosome dynamics to regulate daughter cell fate.Nature communications · 2025Article
- Article
- Adhesion molecule Amigo2 is involved in the fasciculation process of the fasciculus retroflexus.Developmental dynamics : an official publication of the American Association of Anatomists · 2022Article
- The AMIGO1 adhesion protein activates Kv2.1 voltage sensors.Biophysical journal · 2022Article
- Polarized endosome dynamics engage cytoplasmic Par-3 that recruits dynein during asymmetric cell division.Science advances · 2021Article
- Article
- Article
- Regenerative Potential of Carbon Monoxide in Adult Neural Circuits of the Central Nervous System.International journal of molecular sciences · 2020Review
- AMIGO2 Scales Dendrite Arbors in the Retina.Cell reports · 2019Article
- Histone H4 acetylation regulates behavioral inter-individual variability in zebrafish.Genome biology · 2018Article
- Kv2 Ion Channels Determine the Expression and Localization of the Associated AMIGO-1 Cell Adhesion Molecule in Adult Brain Neurons.Frontiers in molecular neuroscience · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Amigo protein family consists of three transmembrane proteins characterized by six leucine-rich repeat domains and one immunoglobulin-like domain in their extracellular moieties. Previous in vitro studies have suggested a role as homophilic adhesion molecules in brain neurons, but the in vivo functions remain unknown. Here we have cloned all three zebrafish amigos and show that amigo1 is the predominant family member expressed during nervous system development in zebrafish. Knockdown of amigo1 expression using morpholino oligonucleotides impairs the formation of fasciculated tracts in early fiber scaffolds of brain. A similar defect in fiber tract development is caused by mRNA-mediated expression of the Amigo1 ectodomain that inhibits adhesion mediated by the full-length protein. Analysis of differentiated neural circuits reveals defects in the catecholaminergic system. At the behavioral level, the disturbed formation of neural circuitry is reflected in enhanced locomotor activity and in the inability of the larvae to perform normal escape responses. We suggest that Amigo1 is essential for the development of neural circuits of zebrafish, where its mechanism involves homophilic interactions within the developing fiber tracts and regulation of the Kv2.1 potassium channel to form functional neural circuitry that controls locomotion.
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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.