Neurofilament-L (NF-L), one subunit of the neuronal intermediate filaments, is a major element of neuronal cytoskeletons. The dynamics of NF-L are regulated by phosphorylation of its head domain. The phosphorylation sites of the NF-L head domain by protein kinase A, protein kinase C, and Rho- associated kinase have been previously identified, and those by calcium/calmodulin-dependent protein kinase II (CaMKII) were identified in this study. A series of site- and phosphorylation state-specific antibodies against NF-L was prepared to investigate NF-L phosphorylation in neuronal systems. Long-term potentiation (LTP) is a cellular model of neuronal plasticity that is thought to involve the phosphorylation of various proteins. NF-L is considered a possible substrate for phosphorylation. During LTP stimulation of mouse hippocampal slices, the series of antibodies demonstrated the increase in the phosphorylation level of Ser57 in NF-L and the visualization of the localized distribution of Ser57 phosphorylation in a subpopulation of apical dendrites of the pyramidal neurons. Furthermore, Ser57 phosphorylation during LTP is suggested to be mediated by CaMKII. Here we show that NF-L is phosphorylated by CaMKII in a subpopulation of apical dendrites during LTP, indicating that Ser57 is a novel phosphorylation site of NF-L in vivo related to the neuronal signal transduction.
|Number of pages||10|
|Journal||Journal of neurochemistry|
|Publication status||Published - 2000|
All Science Journal Classification (ASJC) codes
- Cellular and Molecular Neuroscience