Reeler domain is a protein domain. Extracellular matrix (ECM) proteins play an important role in early cortical development, specifically in the formation of neural connections and in controlling the cytoarchitecture of the central nervous system. The product of the reeler gene in mouse is reelin, a large extracellular protein secreted by pioneer neurons that coordinates cell positioning during neurodevelopment.[1] F-spondin and mindin are a family of matrix-attached adhesion molecules that share structural similarities and overlapping domains of expression. Both F-spondin and mindin promote adhesion and outgrowth of hippocampal embryonic neurons and bind to a putative receptor(s) expressed on both hippocampal and sensory neurons.[2]
This domain of unknown function is found at the N terminus of reelin and F-spondin.
Examples
Human genes that encode proteins containing the reeler domain include:
References
- ^ Cooper JA, Nakajima K, Mikoshiba K, Curran T, Sheldon M, Rice DS, D'Arcangelo G, Yoneshima H, Howell BW, Goldowitz D (1997). "Scrambler and yotari disrupt the disabled gene and produce a reeler-like phenotype in mice". Nature. 389 (6652): 730–733. Bibcode:1997Natur.389..730S. doi:10.1038/39601. PMID 9338784. S2CID 4414738.
- ^ Okamoto H, Higashijima S, Garcia C, Feinstein Y, Borrell V, Burstyn-Cohen T, Tzarfaty V, Frumkin A, Nose A, Soriano E, Klar A (1999). "F-spondin and mindin: two structurally and functionally related genes expressed in the hippocampus that promote outgrowth of embryonic hippocampal neurons". Development. 126 (16): 3637–3648. doi:10.1242/dev.126.16.3637. PMID 10409509.
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This page was last edited on 12 May 2024, at 16:23