Evidence map›Paper›PMID 7721944›Full record

ArticleThe Journal of cell biology1995

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

T Nakagawa, J Chen, Z Zhang, Y Kanai, N Hirokawa

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 114 citations in OpenAlex.

  1. Neurofilaments in health and Charcot-Marie-Tooth disease.Frontiers in cell and developmental biology · 2023
    Review
  2. Review
  3. Chemotherapy-Induced Peripheral Neuropathy and Changes in Cytoskeleton.International journal of molecular sciences · 2019
    Review
  4. Article
  5. Neurofilaments and Neurofilament Proteins in Health and Disease.Cold Spring Harbor perspectives in biology · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phosphorylation of highly conserved neurofilament medium KSP repeats is not required for myelin-dependent radial axonal growth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  14. Article
  15. Neurotrophins and peripheral neuropathies.Brain pathology (Zurich, Switzerland) · 2006
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Neurofilament transport in vivo minimally requires hetero-oligomer formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

T NakagawaDepartment of Anatomy and Cell Biology, University of Tokyo, Faculty of Medicine, Japan.
J Chen
Z Zhang
Y Kanai
N Hirokawa
Tokyo University of Agriculture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurofilaments are the major cytoskeletal elements in the axon that take highly ordered structures composed of parallel arrays of 10-nm filaments linked to each other with frequent cross-bridges, and they are believed to maintain a highly polarized neuronal cell shape. Here we report the function of rat NF-M in this characteristic neurofilament assembly. Transfection experiments were done in an insect Sf9 cell line lacking endogenous intermediate filaments. NF-L and NF-M coassemble to form bundles of 10-nm filaments packed in a parallel manner with frequent cross-bridges resembling the neurofilament domains in the axon when expressed together in Sf9 cells. Considering the fact that the expression of either NF-L or NF-M alone in these cells results in neither formation of any ordered network of 10-nm filaments nor cross-bridge structures, NF-M plays a crucial role in this parallel filament assembly. In the case of NF-H the carboxyl-tail domain has been shown to constitute the cross-bridge structures. The similarity in molecular architecture between NF-M and NF-H suggests that the carboxyl-terminal tail domain of NF-M also constitutes cross-bridges. To examine this and to further investigate the function of the carboxyl-terminal tail domain of NF-M, we made various deletion mutants that lacked part of their tail domains, and we expressed these with NF-L. From this deletion mutant analysis, we conclude that the carboxyl-terminal tail domain of NF-M has two distinct functions. First, it is the structural component of cross-bridges, and these cross-bridges serve to control the spacing between core filaments. Second, the portion of the carboxyl-terminal tail domain of NF-M that is directly involved in cross-bridge formation affects the core filament assembly by helping them to elongate longitudinally so that they become straight.

Indexed as

Amino Acid SequenceAnimalsBaculoviridaeBase SequenceCell LineCytoskeletonGenetic VectorsModels, BiologicalMolecular Sequence DataNeurofilament ProteinsProto-Oncogene Proteins c-mycRatsSequence DeletionSpodopteraneurofilament protein Lneurofilament protein MNeurofilament ProteinsProto-Oncogene Proteins c-myc

Identifiers

PMID7721944
PMCPMC2199923
OpenAlexW2145229125

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.