Axonal Transport: Each Major Rate Component Reflects the Movement of Distinct Macromolecular Complexes
- 9 October 1981
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 214 (4517), 179-181
- https://doi.org/10.1126/science.6169148
Abstract
The proteins of the three major rate components of axonal transport in guinea pig retinal ganglion cells were analyzed by one- and two-dimensional gel electrophoresis. Each rate component consisted of a different set of proteins that remained associated with each other during transport. This suggests that each rate component represents a distinct macromolecular complex and that these complexes may be definable organelles such as microtubules, microfilaments, and smooth endoplasmic reticulum. Thus, the transport of radiolabeled proteins in the axon reflects the movement of complete subcellular rather than the movement of individual proteins.Keywords
This publication has 30 references indexed in Scilit:
- Clathrin is axonally transported as part of slow component b: the microfilament complex.The Journal of cell biology, 1981
- Slow components of axonal transport: two cytoskeletal networks.The Journal of cell biology, 1980
- The movement of membranous organelles in axons. Electron microscopic identification of anterogradely and retrogradely transported organelles.The Journal of cell biology, 1980
- Axonal transport of actin in rabbit retinal ganglion cells.The Journal of cell biology, 1979
- A difference between the proteins conveyed in the fast component of axonal transport in guinea pig hypoglossal and vagus motor neuronsJournal of Neurobiology, 1978
- Axonal inclusions in the crabHemigrapsus nudusJournal of Neurocytology, 1978
- Quantitative Film Detection of 3H and 14C in Polyacrylamide Gels by FluorographyEuropean Journal of Biochemistry, 1975
- Retrograde intraaxonal transport of horseradish peroxidase in retinal ganglion cells of the chickBrain Research, 1975
- Thiol groups of liver alcohol dehydrogenase. Accessibility to general thiol reagents and to potential affinity‐labelsFEBS Letters, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970