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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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In vitro assay of neurofilament light chain self-assembly using truncated mutants

Cited 5 times inthomson ciCited 5 times inthomson ci
Title
In vitro assay of neurofilament light chain self-assembly using truncated mutants
Author
Kim, Sung-KukCho, Sang-MinLee, In-BumLee, Young HanKang, Jung HoonChoi, Jang HyunSuh, Pann-GhillChang, Jong-Soo
Keywords
Electron microscopy; GST pull-down; Neurofilament light chain; PC12 cells; Self-assembly assay; SW13 cells; Turbidity; Western blotting
Issue Date
200704
Publisher
ELSEVIER SCIENCE BV
Citation
JOURNAL OF NEUROSCIENCE METHODS, v.161, no.2, pp.199 - 204
Abstract
Neurofilaments (NFs) are heteropolymers composed of light (NF-L), middle (NF-M), and heavy (NF-H) subunits, present in most neurons. NF-L polymerizes on its own to provide a scaffold on which regular NFs form via the cross-bridging of NF-M or NF-H. To clarify the mechanism of regulation of NF-L self-assembly, we developed an assay using truncated mutant NF-L fused to glutathione-S transferase (GST). Western immunoblotting data show that the GST-fused head-rod domains of NF-L are necessary and sufficient for detecting assembled NF-L. The levels of self-assembled NF-L subunits detected using GST fusion proteins were consistent with those detected by electron microscopy and turbidity assay. Our results collectively imply that GST-fused head-rod domains of NF-L are critical tools for analyzing NF-L self-assembly in vitro.
URI
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DOI
http://dx.doi.org/10.1016/j.jneumeth.2006.10.022
ISSN
0165-0270
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