ArticleProceedings of the National Academy of Sciences of the United States of America1997
Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- Astroglial heme oxygenase-1 and the origin of corpora amylacea in aging and degenerating neural tissues.Experimental neurology · 2014Article
- Development and application of STEM for the biological sciences.Ultramicroscopy · 2012Review
- Amyloid structure and assembly: insights from scanning transmission electron microscopy.Journal of structural biology · 2011Review
- Physical model for the width distribution of axons.The European physical journal. E, Soft matter · 2009Article
- Mass of the postsynaptic density and enumeration of three key molecules.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Mass distribution and spatial organization of the linear bacterial motor of Spiroplasma citri R8A2.Journal of bacteriology · 2003Article
- Relating interactions between neurofilaments to the structure of axonal neurofilament distributions through polymer brush models.Biophysical journal · 2002Article
- Association of actin filaments with axonal microtubule tracts.Journal of neurocytology · 1999Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation plays a critical role in controlling the function of cytoskeletal assemblies but no direct method yet exists to measure the phosphorylation state of proteins at the level of individual molecules and assemblies. Herein, we apply scanning transmission electron microscopy in combination with electron energy loss spectroscopy to measure the distributions of mass and phosphorus in neurofilaments (NFs) isolated from the squid giant axon. We find that native squid NFs, in contrast to typical reconstituted intermediate filaments, are a relatively homogeneous population containing only eight coiled-coil dimers per cross section. The measured stoichiometry of approximately 1:1 for light/heavy peptides strongly suggests that squid NFs are composed of heterodimers. Furthermore, each heavy chain of the dimers carries at least 100 phosphate groups and is, therefore, near-maximally phosphorylated. These results also demonstrate that scanning transmission electron microscopy combined with electron energy loss spectroscopy at the nanometer scale is capable of characterizing the level and distribution of phosphorylation in individual mass-mapped protein assemblies.
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