ArticleCellular and molecular neurobiology2000
Tubulin and neurofilament proteins are transported differently in axons of chicken motoneurons.
Article in Cellular and molecular neurobiology, 2000. 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, 12 citations in OpenAlex.
- The active Hsc70/tau complex can be exploited to enhance tau turnover without damaging microtubule dynamics.Human molecular genetics · 2015Article
- Isoform-selective Genetic Inhibition of Constitutive Cytosolic Hsp70 Activity Promotes Client Tau Degradation Using an Altered Co-chaperone Complement.The Journal of biological chemistry · 2015Article
- Article
- S-nitrosation of proteins: An emergent regulatory mechanism in microvascular permeability and vascular function.Tissue barriers · 2013Article
- Neurofilaments form a highly stable stationary cytoskeleton after reaching a critical level in axons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Alpha-internexin is structurally and functionally associated with the neurofilament triplet proteins in the mature CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Neurofilament transport in vivo minimally requires hetero-oligomer formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Myosin Va binding to neurofilaments is essential for correct myosin Va distribution and transport and neurofilament density.The Journal of cell biology · 2002Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. We previously showed that actin is transported in an unassembled form with its associated proteins actin depolymerizing factor, cofilin, and profilin. Here we examine the specific activities of radioactively labeled tubulin and neurofilament proteins in subcellular fractions of the chicken sciatic nerve following injection of L-[35S]methionine into the lumbar spinal cord. 2. At intervals of 12 and 20 days after injection, nerves were cut into 1-cm segments and separated into Triton X-100-soluble and particulate fractions. Analysis of the fractions by high-resolution two-dimensional gel electrophoresis, immunoblotting, fluorography, and computer densitometry showed that tubulin was transported as a unimodal wave at a slower average rate (2-2.5 mm/day) than actin (4-5 mm/day). Moreover, the specific activity of soluble tubulin was five times that of its particulate form, indicating that tubulin is transported in a dimeric or small oligomeric form and is assembled into stationary microtubules. 3. Neurofilament triplet proteins were detected only in the particulate fractions and transported at a slower average rate (1 mm/day) than either actin or tubulin. 4. Our results indicate that the tubulin was transported in an unpolymerized form and that the neurofilament proteins were transported in an insoluble, presumably polymerized form.
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