ArticleThe Journal of cell biology1994
Differential dynamics of neurofilament-H protein and neurofilament-L protein in neurons.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 60 citations in OpenAlex.
- Parallel Cerebrospinal Fluid and Serum Temporal Profile Assessment of Axonal Injury Biomarkers Neurofilament-Light Chain and Phosphorylated Neurofilament-Heavy Chain: Associations With Patient Outcome in Moderate-Severe Traumatic Brain Injury.Journal of neurotrauma · 2024Article
- A critical reevaluation of the stationary axonal cytoskeleton hypothesis.Cytoskeleton (Hoboken, N.J.) · 2013Review
- Secretin receptor promotes the proliferation of endocrine tumor cells via the PI3K/AKT pathway.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Neurofilament transport in vivo minimally requires hetero-oligomer formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Live-cell imaging of slow axonal transport in cultured neurons.Methods in cell biology · 2003Article
- Rapid intermittent movement of axonal neurofilaments observed by fluorescence photobleaching.Molecular biology of the cell · 2001Article
- Neurofilaments consist of distinct populations that can be distinguished by C-terminal phosphorylation, bundling, and axonal transport rate in growing axonal neurites.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
- Glutamate slows axonal transport of neurofilaments in transfected neurons.The Journal of cell biology · 2000Article
- Kinesin superfamily protein 3 (KIF3) motor transports fodrin-associating vesicles important for neurite building.The Journal of cell biology · 2000Article
- Slow transport of unpolymerized tubulin and polymerized neurofilament in the squid giant axon.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Slow axonal transport of neurofilament protein in cultured neurons.The Journal of cell biology · 1999Article
- Oligodendroglia regulate the regional expansion of axon caliber and local accumulation of neurofilaments during development independently of myelin formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1996Article
- Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross-bridge formation and longitudinal elongation of filaments.The Journal of cell biology · 1995Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neurofilaments (NFs) are composed of triplet proteins, NF-H, NF-M, and NF-L. To understand the dynamics of NFs in vivo, we studied the dynamics of NF-H and compared them to those of NF-L, using the combination of microinjection technique and fluorescence recovery after photobleaching. In the case of NF-L protein, the bleached zone gradually restored its fluorescence intensity with a recovery half time of approximately 35 min. On the other hand, recovery of the bleached zone of NF-H was considerably faster, taking place in approximately 19 min. However, in both cases the bleached zone was stationary. Thus, it was suggested that NF-H is the dynamic component of the NF array and is interchangeable, but that it assembles with the other neurofilament triplet proteins in a more exchangeable way, implying that the location of NF-H is in the periphery of the core NF array mainly composed of NF-L subunits. Immunoelectron microscopy investigations of the incorporation sites of NF-H labeled with biotin compounds also revealed the lateral insertion of NF-H subunits into the preexisting NF array, taking after the pattern seen in the case of NF-L. In summary, our results demonstrate that the dynamics of the L and H subunit proteins in situ are quite different from each other, suggesting different and separated mechanisms or structural specialization underlying the behavior of the two proteins.
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