ArticleOpen biology2016
Structure of astrotactin-2: a conserved vertebrate-specific and perforin-like membrane protein involved in neuronal development.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
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- Deep Transcriptomic Analysis Reveals the Dynamic Developmental Progression during Early Development of Channel Catfish (International journal of molecular sciences · 2020Article
- Structure and mechanism of bactericidal mammalian perforin-2, an ancient agent of innate immunity.Science advances · 2020Article
- Investigation of gene-gene interactions in cardiac traits and serum fatty acid levels in the LURIC Health Study.PloS one · 2020Article
- Deep mixed model for marginal epistasis detection and population stratification correction in genome-wide association studies.BMC bioinformatics · 2019Article
- The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1.Nature communications · 2019Article
- Murine astrotactins 1 and 2 have a similar membrane topology and mature via endoproteolytic cleavage catalyzed by a signal peptidase.The Journal of biological chemistry · 2019Article
- ASTN2 modulates synaptic strength by trafficking and degradation of surface proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structures of monomeric and oligomeric forms of theScience advances · 2018Article
- Repurposing a pore: highly conserved perforin-like proteins with alternative mechanisms.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Intramembrane Proteolysis of Astrotactins.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The vertebrate-specific proteins astrotactin-1 and 2 (ASTN-1 and ASTN-2) are integral membrane perforin-like proteins known to play critical roles in neurodevelopment, while ASTN-2 has been linked to the planar cell polarity pathway in hair cells. Genetic variations associated with them are linked to a variety of neurodevelopmental disorders and other neurological pathologies, including an advanced onset of Alzheimer's disease. Here we present the structure of the majority endosomal region of ASTN-2, showing it to consist of a unique combination of polypeptide folds: a perforin-like domain, a minimal epidermal growth factor-like module, a unique form of fibronectin type III domain and an annexin-like domain. The perforin-like domain differs from that of other members of the membrane attack complex-perforin (MACPF) protein family in ways that suggest ASTN-2 does not form pores. Structural and biophysical data show that ASTN-2 (but not ASTN-1) binds inositol triphosphates, suggesting a mechanism for membrane recognition or secondary messenger regulation of its activity. The annexin-like domain is closest in fold to repeat three of human annexin V and similarly binds calcium, and yet shares no sequence homology with it. Overall, our structure provides the first atomic-resolution description of a MACPF protein involved in development, while highlighting distinctive features of ASTN-2 responsible for its activity.
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