Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly.
10.3858/emm.2011.43.3.019
- Author:
Sung Kuk KIM
1
;
Ho KIM
;
Yong Ryoul YANG
;
Pann Ghill SUH
;
Jong Soo CHANG
Author Information
1. Department of Life Science, College of Natural Science, Daejin University, Kyeonggido 487-711, Korea. jchang@daejin.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
neurofilament protein L;
phosphatidylinositol phosphates;
phospholipase Cgamma
- MeSH:
Animals;
Fluorescent Antibody Technique;
Mice;
Mutation/genetics;
Neurofilament Proteins/genetics/*metabolism;
Phosphatidylinositol Phosphates/*metabolism;
Phospholipase C gamma/metabolism;
*Protein Multimerization
- From:Experimental & Molecular Medicine
2011;43(3):153-160
- CountryRepublic of Korea
- Language:English
-
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.
