PhosphoPlus® NeuroD1 (Ser274) Antibody Duet #66212
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Background
Erk1/2 kinase activity is stimulated by glucose and calcium influx in pancreatic beta cells, and the subsequent phosphorylation of NeuroD1 at Ser274 promotes insulin gene transcription (7,8). Phosphorylated NeuroD1 in the pancreas is increasingly translocated to the nucleus, where it directly interacts with the insulin promoter (9). Active, nuclear NeuroD1 acts in synergy with Pdx1 to activate insulin, NKX2.2, and islet amyloid polypeptide (IAPP) transcription while suppressing Pdx1-driven transcription of somatostatin (10,11). In developing rat pineal gland, phosphorylation of NeuroD1 at Ser274 and Ser336 is tightly correlated with NeuroD1 nuclear localization, and cytoplasmic to nuclear shuttling of the protein is under cyclical day and night adrenergic control (12). In 293T cells, transfection of a nonphosphorylatable Ser274Ala mutant blocked NeuroD1 ubiquitination and proteasomal degradation (13). The localization of phosphorylated NeuroD1 is reversed in these cells compared to pancreatic beta cells, with a Ser274Glu phospho-mimic localized primarily to the cytoplasm in the former, further evidence of the context-specific nature of this modification. (13).
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- Lee, T.Y. et al. (2020) Exp Neurobiol 29, 189-206.
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