A real gene for reeler

Article Abstract:

G. D'Arcangelo and colleagues has discovered the full-length complementary DNA that is responsible for the reeler mutation which involves abnormal corticogenesis and whose mechanism was previously unknown. They were able to deduce a protein called reelin which matches the features of a secreted extracellular protein and which has 3,461 residues. Reelin RNA is 12 kilobases long and is first detected on day 11.5 of an embryonic brain. The protein is most likely involved in architectonic cell pattern stabilization. The reeler gene is present in human but is likely fatal since no known disorder is tied to that location.

Proteins, Mutation (Biology), Mutation

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Decoding the Reelin signal

Article Abstract:

It has been established that mice without both the very low density lipoprotein (VLDL) receptor and apolipoprotein E receptor-2 genes show the same characteristics as mice lacking Reelin, a large glycoprotein found in the extracellular matrix. Reelin is secreted by, and surrounds, cells. The finding that Reelin, Dab1 and the VLDL receptor/ApoE-R2 act in the same genetic pathway is well aligned with previous observations. It is possible that the VLDL receptor and ApoE-R2 are receptors to Reelin or fragments of this protein.

Genetic aspects, Mice, Mice (Rodents), Neurotransmitter receptors

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Unscrambling a disabled brain

Article Abstract:

The mouse disabled homologue 1 (mdab1) gene is a vital element of the Reelin response in target neuronal cells. Extracellular Reelin signals to nearby neurons by activating a kinase cascade. There is still uncertainty about the transcriptional mechanisms that regulate Reelin expression. Furthermore, little is known about how Reelin acts on target neurons. There may be a surface Reelin receptor linked with intracellular transduction, or Reelin may interact less directly with other receptor systems.

Physiological aspects, Neurons, Neural circuitry

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