PMID: 9166753Jun 1, 1997Paper

Increased solubility of high-molecular-mass neurofilament subunit by suppression of dephosphorylation: its relation to axonal transport

Journal of Neurochemistry
M TsudaY Komiya

Abstract

To investigate the role of phosphorylation in the turnover and transport of neurofilament (NF) proteins in vivo, we studied their solubility properties and axonal transport in the rat sciatic nerve using phosphatase inhibitors to minimize dephosphorylation during preparation. About 20% of the 200-kDa subunit (NF-H) in the axon was soluble in the 1% Triton-containing buffer under the present conditions, whereas this amount was less and more variable in the absence of phosphatase inhibitors. The 68-kDa subunit (NF-L) was exclusively insoluble and not affected by the inhibitors. Such selective solubilization of NF-H by phosphorylation differed significantly from the in vitro phosphorylation with cyclic AMP-dependent protein kinase, which resulted in NF disassembly. The carboxy-terminal phosphorylation state of NF-H probed with the phosphorylation-sensitive antibodies was also not directly related to solubility. The solubility of NF-H did not differ along the nerve. In contrast, the solubility of L-[35S]methionine-labeled, transported NF-H was lowest at the peak of radioactivity. Higher solubility at the leading edge, regardless of its location along the nerve, indicates that NF-H solubility is positively correlated with the rate o...Continue Reading

Citations

Apr 12, 2000·Journal of Neuropathology and Experimental Neurology·S X ZhangJ W Geddes
Jan 15, 2004·Journal of Neurochemistry·Atsuko UchidaShin-ichi Hisanaga
Apr 1, 2000·Cell Motility and the Cytoskeleton·J T YabeT B Shea
Feb 14, 2006·Neurochemical Research·Fuyong SongKeqin Xie
May 8, 2001·Journal of Neuroscience Research·A UchidaS Hisanaga
Mar 4, 1998·Current Opinion in Cell Biology·R A Nixon
Jun 23, 2004·Toxicology and Applied Pharmacology·Richard M LoPachinLisa A Opanashuk
May 4, 2007·BMC Neuroscience·Nadia TagnaoutiMatthias Kneussel

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