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

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Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly

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Title
Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly
Author
Kim, Sung-KukKim, HoYang, Yong-RyoulSuh, Pann-GhillChang, Jong-Soo
Keywords
Neurofilament protein L; Phosphatidylino-sitol phosphates; Phospholipase Cγ
Issue Date
2011-03
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Citation
EXPERIMENTAL AND MOLECULAR MEDICINE, v.43, no.3, pp.153 - 160
Abstract
Phosphatidylinositol phosphates (PtdlnsPs) are ubiquitous membrane phospholipids that play diverse roles in cell growth and differentiation. To clarify the regulation mechanism acting on neurofilament light chain (NF-L) self assembly, we examined the effects of various PtdlnsPs on this process. We found that PtdlnsPs, including Pl(4,5)P(2), directly bind to the positively charged Arg(54) of murine NF-L, and this binding promotes NF-L self assembly in vitro. Mutant NF-L (R53A/R54A) proteins lacking binding affinity to PtdlnsPs did not have the same effect, but the mutant NF-L proteins showed greater self assembly than the wild-type in the absence of any PtdlnsP. These results collectively suggest that Arg54 plays a pivotal role in NF-L self assembly by binding with PtdlnsPs.
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DOI
10.3858/emm.2011.43.3.019
ISSN
1226-3613
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SLS_Journal Papers
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