Phosphatidylinositol phosphates directly bind to neurofilament light chain (NF-L) for the regulation of NF-L self assembly
Experimental & Molecular Medicine
;
: 153-160, 2011.
Article
in English
| WPRIM
| ID: wpr-171913
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Fluorescent Antibody Technique
/
Neurofilament Proteins
/
Phosphatidylinositol Phosphates
/
Phospholipase C gamma
/
Protein Multimerization
/
Mutation
Limits:
Animals
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2011
Type:
Article
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