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• W2054013596 abstract "Neurofilaments (NFs) are neuron-specific intermediate filaments (IFs) composed of three different subunits, NF-L, NF-M, and NF-H. NFs move down the axon with the slow component of axonal transport, together with microtubules, microfilaments, and αII/βII-spectrin (nonerythroid spectrin or fodrin). It has been shown that αII/βII-spectrin is closely associated with NFs in vivo and that βII-spectrin subunit binds to NF-L filaments in vitro. In the present study we seek to elucidate the relationship between NF-L and βII-spectrin in vivo. We transiently transfected full-length NF-L and carboxyl-terminal deleted NF-L mutants in SW13 Cl.2 Vim − cells, which lack an endogenous IF network and express αII/βIIΣ1-spectrin. Double-immunofluorescence and electron microscopy studies showed that a large portion of βIIΣ1-spectrin colocalizes with the structures formed by NF-L proteins. We found a similar association between NF-L proteins and actin. However, coimmunoprecipitation experiments in transfected cells and the yeast two-hybrid system results failed to demonstrate a direct interaction of NF-L with βIIΣ1-spectrin in vivo. The presence of another protein that acts as a bridge between the membrane skeleton and neurofilaments or modulating their association may therefore be required." @default.
• W2054013596 created "2016-06-24" @default.
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• W2054013596 date "1999-07-01" @default.
• W2054013596 modified "2023-10-17" @default.
• W2054013596 title "Characterization of NF-L and βIIΣ1-Spectrin Interaction in Live Cells" @default.
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• W2054013596 doi "https://doi.org/10.1006/excr.1999.4479" @default.
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• W2054013596 hasPublicationYear "1999" @default.
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