Neurofilament triplet protein interactions: evidence for the preferred formation of NF-L-containing dimers and a putative function for the end domains.
In this report we examine the molecular interactions that lead to formation of neurofilaments, the intermediate filaments in neurons. Using the yeast two-hybrid system, we found that the rod domains of all three NF triplet proteins interacted strongly with one another and with rod domains of the Type III IF proteins, vimentin and desmin. A slight preference toward NF-L-containing dimers was observed over ones not containing NF-L. Interactions among the full length NF triplet proteins exhibited more specificity. Full length NF-L had only a relatively weak interaction with another full length NF-L molecule, but reacted more robustly with full length NF-M or NF-H lacking only part of the head domain. No homologous or heterologous dimerization of NF-M and NF-H was detectable. These results support the hypothesis that neurofilaments are obligate heteropolymers and that heterodimeric subunits are the preferred building blocks. They further suggest that the mechanism that specifies heterodimeric interaction among the NF triplet proteins resides in the end domains.
Carpenter
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Department of Cell Biology, Neurobiology, and Anatomy, University of Cincinnati College of Medicine, Ohio 45267-0521, USA.
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D001483:Base Sequence; D017931:DNA Primers; D003893:Desmin / Q000378:metabolism; D019281:Dimerization; D016900:Neurofilament Proteins / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D012441:Saccharomyces cerevisiae; D014746:Vimentin / Q000378:metabolism
D017931:DNA Primers; D003893:Desmin; D016900:Neurofilament Proteins; D014746:Vimentin; C044882:neurofilament protein L; C051774:neurofilament protein H; C061195:neurofilament protein M