Interaction domains of neurofilament light chain and brain spectrin.

We have previously demonstrated that brain spectrin binds to the low-molecular-mass subunit of neurofilaments (NF-L) [Frappier, Regnouf & Pradel (1987) Eur. J. Biochem. 169, 651-657]. In the present study, we seek to locate their respective binding domains. In the first part we demonstrate that brain spectrin binds to a 20 ...
kDa domain of NF-L. This domain is part of the rod domain of neurofilaments and plays a role in the polymerization process. However, the polymerization state does not seem to have any influence on the interaction. In the second part, we provide evidence that NF-L binds to the beta-subunit of not only brain spectrin but also human and avian erythrocyte spectrins. The microtubule-associated protein, MAP2, which has also been shown to bind to microfilaments and neurofilaments, binds to the same domain of NF-L as spectrin does. Finally, among the tryptic peptides of brain spectrin, we show that some peptides of low molecular mass (35, 25, 20 and 18 kDa) co-sediment with either NF-L or F-actin.
Mesh Terms:
Animals, Brain, Chickens, Electrophoresis, Polyacrylamide Gel, Erythrocytes, Humans, Intermediate Filament Proteins, Intermediate Filaments, Macromolecular Substances, Microfilaments, Microscopy, Electron, Molecular Weight, Neurofilament Proteins, Protein Binding, Spectrin, Spinal Cord, Swine
Biochem. J.
Date: Apr. 15, 1991
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