title: Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly.
abstract: Phosphatidylinositol phosphates (PtdInsPs) 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 PtdInsPs on this process. We found that PtdInsPs, including PI(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 PtdInsPs 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 PtdInsP. These results collectively suggest that Arg(54) plays a pivotal role in NF-L self assembly by binding with PtdInsPs.
authors.affiliation: Department of Life Science, College of Natural Science, Daejin University, Kyeonggido, Korea.
authors.forename: Sung-Kuk
authors.initials: SK
authors.lastname: Kim
authors.forename: Ho
authors.initials: H
authors.lastname: Kim
authors.forename: Yong-Ryoul
authors.initials: YR
authors.lastname: Yang
authors.forename: Pann-Ghill
authors.initials: PG
authors.lastname: Suh
authors.forename: Jong-Soo
authors.initials: JS
authors.lastname: Chang
mesh_terms: D000818:Animals; D005455:Fluorescent Antibody Technique; D051379:Mice; D009154:Mutation / Q000235:genetics; D016900:Neurofilament Proteins / Q000235:genetics / Q000378:metabolism*; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism*; D051966:Phospholipase C gamma / Q000378:metabolism; D055503:Protein Multimerization
chemical_list: D016900:Neurofilament Proteins; D018129:Phosphatidylinositol Phosphates; C044882:neurofilament protein L; D051966:Phospholipase C gamma