Exp Mol Med.  2011 Mar;43(3):153-160. 10.3858/emm.2011.43.3.019.

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

• Kim SK
• Kim H
• Yang YR
• Suh PG
• Chang JS

• KMID: 1109404
• DOI: http://doi.org/10.3858/emm.2011.43.3.019

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)P2, directly bind to the positively charged Arg54 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 Arg54 plays a pivotal role in NF-L self assembly by binding with PtdInsPs.

Keyword

neurofilament protein L; phosphatidylinositol phosphates; phospholipase Cgamma

MeSH Terms

Animals
Fluorescent Antibody Technique
Mice
Mutation/genetics
Neurofilament Proteins/genetics/*metabolism
Phosphatidylinositol Phosphates/*metabolism
Phospholipase C gamma/metabolism
*Protein Multimerization