Methyl-CpG Binding Protein 2 (MeCP2) was identified based on its affinity for methylated cytosines within DNA. As a chromatin-associated multifunctional protein, MeCP2 has been implicated in regulation of transcription and chromatin structure. Mutations of MeCP2 cause Rett syndrome, which results from neuronal dysfunction and impairment in cognitive and motor functions. Regulation of MeCP2 activity may involve phosphorylation at multiple sites. Ser-421 in MeCP2 is phosphorylated in response to neuronal activity, calcium influx, and is dependent on Cam-KII. Alanine mutation of Ser-421 leads to defects in synapse development and activity. Ser-80 in MeCP2 is phosphorylated in HeLa nuclear extracts and neurons. Alanine mutation of Ser-80 attenuates MeCP2 chromatin association and leads to locomotor deficits in transgenic knock-in mice. Thus, phosphorylation of MeCP2 may be important for altering its function during neuronal activity.
Tao, J. et al. (2009) PNAS 106(12):4882.
Lewis, J.D. et al. (1992). Cell 69:905.
*For more information, see UniProt Accession Q9Z2D6
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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