Stable polymers of the axonal cytoskeleton: the axoplasmic ghost

doi:10.1083/jcb.92.1.192

This Article

	Full Text (PDF, 927K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Morris, J. R.
	Articles by Lasek, R. J.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Morris, J. R.
	Articles by Lasek, R. J.


Social Bookmarking

	What's this?

ARTICLES

Stable polymers of the axonal cytoskeleton: the axoplasmic ghost

JR Morris and RJ Lasek

We have examined the monomer-polymer equilibria which form the cytoskeletal polymers in squid axoplasm by extracting protein at low concentrations of monomer. The solution conditions inside the axon were matched as closely as possible by the extraction buffer (buffer P) to preserve the types of protein associations that occur in axoplasm. Upon extraction in buffer P, all of the neurofilament proteins in axoplasm remain polymerized as part of the stable neurofilament network. In contrast, most of the polymerized tubulin and actin in axoplasm is soluble although a fraction of these proteins also exists as a stable polymer. Thus, the axoplasmic cytoskeleton contains both stable polymers and soluble polymers. We propose that stable polymers, such as neurofilaments, conserve cytoskeletal organization because they tend to remain polymerized, whereas soluble polymers increase the plasticity of the cytoskeleton because they permit rapid and reversible changes in cytoskeletal organization.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Bearer, E. L., Breakefield, X. O., Schuback, D., Reese, T. S., LaVail, J. H. (2000). Retrograde axonal transport of herpes simplex virus: Evidence for a single mechanism and a role for tegument. Proc. Natl. Acad. Sci. USA 97: 8146-8150 [Abstract] [Full Text]
Galbraith, J. A., Reese, T. S., Schlief, M. L., Gallant, P. E. (1999). Slow transport of unpolymerized tubulin and polymerized neurofilament in the squid giant axon. Proc. Natl. Acad. Sci. USA 96: 11589-11594 [Abstract] [Full Text]
Ratner, N., Bloom, G. S., Brady, S. T. (1998). A Role for Cyclin-Dependent Kinase(s) in the Modulation of Fast Anterograde Axonal Transport: Effects Defined by Olomoucine and the APC Tumor Suppressor Protein. J. Neurosci. 18: 7717-7726 [Abstract] [Full Text]
Guillaud, L., Bosc, C., Fourest-Lieuvin, A., Denarier, E., Pirollet, F., Lafanechere, L., Job, D. (1998). STOP Proteins are Responsible for the High Degree of Microtubule Stabilization Observed in Neuronal Cells. JCB 142: 167-179 [Abstract] [Full Text]
Tabb, J., Molyneaux, B., Cohen, D., Kuznetsov, S., Langford, G. (1998). Transport of ER vesicles on actin filaments in neurons by myosin V. J. Cell Sci. 111: 3221-3234 [Abstract]
Hoffman, P. N. (1995). Review : The Synthesis, Axonal Transport, and Phosphorylation of Neurofilaments Determine Axonal Caliber in Myelinated Nerve Fibers. Neuroscientist 1: 76-83 [Abstract]
Lasek, R.J., Oblinger, M.M., Drake, P.F. (1983). Molecular Biology of Neuronal Geometry: Expression of Neurofilament Genes Influences Axonal Diameter. Cold Spring Harb Symp Quant Biol 48: 731-744 [Abstract]
Allen, R., Metuzals, J, Tasaki, I, Brady, S., Gilbert, S. (1982). Fast axonal transport in squid giant axon. Science 218: 1127-1129 [Abstract]
Brady, S., Lasek, R., Allen, R. (1982). Fast axonal transport in extruded axoplasm from squid giant axon. Science 218: 1129-1131 [Abstract]