sDMA, symmetrical arginine dimethylation

Publication Title: 
Cell Cycle (Georgetown, Tex.)

Abnormal protein interactions of mutant huntingtin (Htt) triggered by polyglutamine expansion are thought to mediate Huntington's disease (HD) pathogenesis. Here, we explored a functional interaction of Htt with protein arginine methyltransferase 5 (PRMT5), an enzyme mediating symmetrical dimethylation of arginine (sDMA) of key cellular proteins, including histones, and spliceosomal Sm proteins. Gene transcription and RNA splicing are impaired in HD. We demonstrated PRMT5 and Htt interaction and their co-localization in transfected neurons and in HD brain.

Author(s): 
Ratovitski, Tamara
Arbez, Nicolas
Stewart, Jacqueline C.
Chighladze, Ekaterine
Ross, Christopher A.
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