Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4329109 | Brain Research | 2008 | 5 Pages |
The carboxyl terminal “tail” domains of the heavy and middle molecular weight mammalian neurofilament (NF) proteins regulate inter-NF spacing and formation of organized networks. The C-terminal region of the larger of the two lamprey NF subunits (NF-180) resembles these mammalian proteins in that it consists of a proximal glutamate-rich region and a distal region containing multiple phosphorylation sites. To investigate the role of these two sidearm domains in the organization of lamprey NFs, we generated plasmids lacking the glutamate-rich domain, the domain containing multiple phosphorylation sites, or both, and examined the impact of the resultant mutant proteins on the endogenous NF network in differentiated NB21/d1 neuroblastoma cells. We present evidence that, like mammalian NFs, the glutamate-rich region of NF-180 sidearm plays a critical role in NF architecture.