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KMID : 0620920110430030153
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Experimental & Molecular Medicine
2011 Volume.43 No. 3 p.153 ~ p.160
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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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Kim Sung-Kuk
Kim Ho
Yang Yong-Ryoul
Suh Pann-Ghill
Chang Jong-Soo
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Abstract
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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.
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KEYWORD
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neurofilament protein L, phosphatidylinositol phosphates, phospholipase Cγ
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