Discrete soluble forms of middle and high molecular weight neurofilament proteins in dilute aqueous buffers.

Neurofilaments and microtubules are important components of the neuronal cytoskeleton. In axons or dendrites, these filaments are aligned in parallel arrays, and separated from one another by nonrandom distances. This distinctive organization has been attributed to cross bridges formed by NF side arms or microtubule-associated proteins. We recently proposed a polymer-brush-based mechanism for regulating interactions between neurofilaments and between microtubules. In this model, the side arms of neurofilaments and the projection domains of microtubule-associated proteins are highly unstructured and exert long-range repulsive forces that are largely entropic in origin; these forces then act to organize the cytoskeleton in axons and dendrites. Here, we review the biochemical, biophysical, genetic and cell biological data for the polymer-brush and cross-bridging models. We explore how the data traditionally used to support cross bridging may be reconciled with a polymer-brush mechanism and compare the implications of recent experimental insights into axonal transport and physiology for each model.

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Molecular mechanisms for organizing the neuronal cytoskeleton

Mukhopadhyay

Kumar

Hoh

2004

BioEssays

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The structure and organization of the human heavy neurofilament subunit (NF-H) and the gene encoding it.

et al. 1988

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Genomic clones for the largest human neurofilament protein (NF‐H) were isolated, the intron/exon boundaries mapped and the entire protein‐coding regions (exons) sequenced. The predicted protein contains a central region that obeys the structural criteria identified for alpha‐helical ‘rod’ domains typically present in all IF protein components: it is approximately 310 amino acids long, shares amino acid sequence homology with other IF protein rod domains and displays the characteristic heptad repeats of apolar amino acids which facilitate coiled‐coil interaction. Nevertheless, anomalies are noted in the structure of the NF‐H rod which could explain observations of its poor homopolymeric assembly in vitro. The protein segment on the carboxy‐terminal side of the human NF‐H rod is uniquely long (greater than 600 amino acids) compared to other IF proteins and is highly charged (greater than 24% Glu, greater than 25% Lys), rich in proline (greater than 12%) and impoverished in cysteine, methionine and aromatic amino acids. Its most remarkable feature is a repetitive sequence that covers more than half its length and includes the sequence motif, Lys‐Ser‐Pro (KSP) greater than 40 times. Together with the recent identification of the serine in KSP as the main target for NF‐directed protein kinases in vivo, this repetitive character explains the massive phosphorylation of the NF‐H subunit that can occur in axons. The human NF‐H gene has three introns, two of which interrupt the protein‐coding sequence at identical points to introns in the genes for the two smaller NF proteins, NF‐M and NF‐L.(ABSTRACT TRUNCATED AT 250 WORDS)

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Early and late appearance of neurofilament phosphorylated epitopes in rat nervous system development: In vivo and in vitro study with monoclonal antibodies

Dahl

1988

J of Neuroscience Research

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Neurofilament phosphorylation in rat nervous system development was studied by indirect immunofluorescence with monoclonal antibodies reacting with phosphorylated epitopes in tissue sections and in primary dissociated cultures. The antibodies either decorated neurofilaments shortly after their appearance or after a considerable delay (from 4 to 9 days in vivo and from 12 to 27 days in vitro), thus suggesting the existence of at least two classes of phosphorylated epitopes. With most antibodies there was a good correlation between in vivo and in vitro findings as to the early or late appearance of phosphorylated epitopes. Monoclonal NE14 was the main exception in that immunoreactivity with this antibody was present in 1-day cultures, while it only occurred 4 days after the first appearance of neurofilaments in vivo. The effect of phosphorylation on neurofilament structure and function remains to be determined. Neurofilament expression is an early phenomenon in ontogeny coinciding with neuronal differentiation. It is possible that late phosphorylation events may stabilize the axonal cytoskeleton following the massive loss of axons that occurs in several fiber tracts during late fetal and neonatal life.

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Discrete soluble forms of middle and high molecular weight neurofilament proteins in dilute aqueous buffers.

Cited by 16 publications

References 47 publications

Molecular mechanisms for organizing the neuronal cytoskeleton

Molecular mechanisms for organizing the neuronal cytoskeleton

The structure and organization of the human heavy neurofilament subunit (NF-H) and the gene encoding it.

Early and late appearance of neurofilament phosphorylated epitopes in rat nervous system development: In vivo and in vitro study with monoclonal antibodies

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