Journal
NEURON
Volume 58, Issue 1, Pages 65-77Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2008.01.037
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Funding
- NICHD NIH HHS [HD18655, P30 HD018655, P30 HD018655-26, P30 HD018655-25] Funding Source: Medline
- NIGMS NIH HHS [T32 GM007753] Funding Source: Medline
- NINDS NIH HHS [T32 NS007473-03, T32 NS007473, P01 NS047572-030001, P01 NS047572-01A10001, R37 NS037116, P01NS047572, P01 NS047572, P01 NS047572-020001, R37NS037116, P01 NS047572-040001, T32 NS007473-04] Funding Source: Medline
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The mechanisms by which proneural basic helix-loop-helix (bHLH) factors control neurogenesis have been characterized, but it is not known how they specify neuronal cell-type identity. Here, we provide evidence that two conserved serine residues on the bHLH factor neurogenin 2 (Ngn2), S231 and S234, are phosphorylated during motor neuron differentiation., In knockin mice in which S231 and S234 of Ngn2 were mutated to alanines, neurogenesis occurs normally, but motor neuron specification is impaired. The phosphorylation of Ngn2 at S231 and S234 facilitates the interaction of Ngn2 with LIM homeodomain transcription factors to specify motor neuron identity. The phosphorylation-dependent cooperativity between Ngn2 and homeodomain transcription factors may be a general mechanism by which the activities of bHLH and homeodomain proteins are temporally and spatially integrated to generate the wide diversity of cell types that are a hallmark of the nervous system.
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