Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments.

Nakagawa, Terunaga; Chen, Jianguo; Zhang, Zhizeng; Kanai, Yoshiyuki; Hirokawa, Nobutaka

doi:10.1083/jcb.129.2.411

Cited by 112 publications

(92 citation statements)

References 45 publications

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“…Variations in caliber size also are closely related to changes in neurofilament protein phosphorylation, which promote the local accumulation of neurofilaments within a stationary, but dynamic, axonal network (Lewis and Nixon, 1988;Nixon et al, 1994a;Takeda et al, 1994) and induce neurofilaments to extend sidearms that increase lateral spacing between neurofilaments (DeWaegh et al, 1992;Hsieh et al, 1994;Nixon et al, 1994b;Nakagawa et al, 1995). Our finding that caliber size does not expand in a proximal portion of optic axons proved to be useful in evaluating the possible contributions of these different neurofilament-related variables to axon radial growth.…”

Section: Local Neurofilament Accumulation and Changes In Neurofilamenmentioning

confidence: 88%

Oligodendroglia Regulate the Regional Expansion of Axon Caliber and Local Accumulation of Neurofilaments during Development Independently of Myelin Formation

Sánchez¹,

Hassinger²,

et al. 1996

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Axon caliber may be influenced by intrinsic neuronal factors and extrinsic factors related to myelination. To understand these extrinsic influences, we studied how axon-caliber expansion is related to changes in neurofilament and microtubule organization as axons of retinal ganglion cells interact with oligodendroglia and become myelinated during normal mouse brain development. Caliber expanded and neurofilaments accumulated only along regions of the axon invested with oligodendroglia. Very proximal portions of axons within a region of the optic nerve from which oligodendrocytes are excluded remained unchanged. More distally, these axons rapidly expanded an average of fourfold as soon as they were recruited to become myelinated between postnatal days 9 and 120. Unmyelinated axons remained unchanged. Axons ensheathed by oligodendroglial processes, but not yet myelinated, were intermediate in caliber and neurofilament number. That oligodendrocytes can trigger regional caliber expansion in the absence of myelin was confirmed using three strains of mice with different mutations that prevent myelin formation but allow wrapping of some axons by oligodendroglial processes. Unmyelinated axons persistently wrapped by oligodendrocytes showed full axon caliber expansion, neurofilament accumulation, and appropriately increased lateral spacing between neurofilaments. Thus, signals from oligodendrocytes, independent of myelin formation, are sufficient to induce full axon radial growth primarily by triggering local accumulation and reorganization of the neurofilament network.

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Section: Local Neurofilament Accumulation and Changes In Neurofilamenmentioning

confidence: 88%

Oligodendroglia Regulate the Regional Expansion of Axon Caliber and Local Accumulation of Neurofilaments during Development Independently of Myelin Formation

Sánchez¹,

Hassinger²,

et al. 1996

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“…Both NF-M and NF-H have unusually long highly charged C-terminal tails that project from the core IF structure (Hirokawa et al, 1997;Hisanaga and Hirokawa, 1988). It has been suggested that these domains, and their modification by phosphorylation, promote filament stability and modify NF transport in axons by regulating interactions with MT and MT-dependent motors (Chen et al, 2000;Hisanaga and Hirokawa, 1988;Jung et al, 2000b;Nakagawa et al, 1995;Yabe et al, 2001b;Yabe et al, 1999). Therefore, it is possible that the tail domains of NF-M and NF-H could be involved, either actively or passively, in determining pause intervals, thereby influencing the total distances traveled by NF.…”

Section: Discussionmentioning

confidence: 99%

Rapid transport of neural intermediate filament protein

Helfand

Loomis

Yoon

et al. 2003

Journal of Cell Science

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Peripherin is a neural intermediate filament protein that is expressed in peripheral and enteric neurons, as well as in PC12 cells. A determination of the motile properties of peripherin has been undertaken in PC12 cells during different stages of neurite outgrowth. The results reveal that non-filamentous, non-membrane bound peripherin particles and short peripherin intermediate filaments, termed `squiggles', are transported at high speed throughout PC12 cell bodies, neurites and growth cones. These movements are bi-directional, and the majority require microtubules along with their associated molecular motors, conventional kinesin and cytoplasmic dynein. Our data demonstrate that peripherin particles and squiggles can move as components of a rapid transport system capable of delivering cytoskeletal subunits to the most distal regions of neurites over relatively short time periods.

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“…Recent transfection experiments (Nakagawa et al, 1995) suggest that the portion of the rat NF-M tail containing phosphorylation sites is critical for proper longitudinal extension of filaments, as well as for cross-bridge formation between adjacent filaments. Analyses of transgenic mice suggest that either NF-M or NF-H, together with NF-L, can stimulate growth of axonal caliber and that interactions beyond those between nearest neighbors are required (Xu et a!., 1996).…”

Section: Discussionmentioning

confidence: 99%

Identification of Ser‐Pro and Thr‐Pro Phosphorylation Sites in Chicken Neurofilament‐M Tail Domain

Bennett

Quintana²

1997

Journal of Neurochemistry

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Abstract:The tail domain of the midsize chicken neurofilament polypeptide (NF-M) contains several different types of Ser-Pro and Thr-Pro putative phosphorylation sites. We determined which of these sites are actually phosphorylated in vivo. Chick sensory neuron cultures were incubated in [ 32P]phosphate, and the cytoskeletal fraction was mixed with a neurofilament fraction prepared from adult chicken brain. NF-M was purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and digested with chymotrypsin, and two large fragments were isolated. These were individually cleaved with trypsin, endoprotease Lys-C, or endoprotease GIu-C, and peptides separated by two-dimensional high-voltage electrophoresis and thin-layer chromatography. 32P-labeled phosphopeptides were eluted from the cellulose plates and subjected to microsequencing and mass spectometry. We found that of 21 potential Ser-Pro and Thr-Pro phosphoacceptor sites, at least 20 are phosphorylated in vivo: all four Lys-Ser-Pro sites and at least 16 of the 17 Lys-Xaa-Xaa-Ser/Thr-Pro repeats. In addition, a novel Ser-Pro site in the extreme carboxy terminus is phosphorylated. This site, which has no proximal Lys residue, is also found in mammalian NF-M, but has not been reported to be phosphorylated. Together with three casein kinase I sites we have found recently in the acidic amino-terminal segment of the tail, a total of 24 or 25 Ser and Thr phosphoacceptor sites have now been located in the chicken NF-M tail.

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Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments.

Cited by 112 publications

References 45 publications

Oligodendroglia Regulate the Regional Expansion of Axon Caliber and Local Accumulation of Neurofilaments during Development Independently of Myelin Formation

Oligodendroglia Regulate the Regional Expansion of Axon Caliber and Local Accumulation of Neurofilaments during Development Independently of Myelin Formation

Rapid transport of neural intermediate filament protein

Identification of Ser‐Pro and Thr‐Pro Phosphorylation Sites in Chicken Neurofilament‐M Tail Domain

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