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Journal of Neuroscience, Vol 16, 531-544, Copyright © 1996 by Society for Neuroscience
Microtubule assembly and turnover in growing axons
Y Li and MM Black
Department of Anatomy and Cell Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
We have shown previously that axonal microtubules (MTs) are composite,
consisting of two distinct domains that differ in their content of
tyrosinated alpha-tubulin (tyr-tub). One domain is poor in tyr-tub and is
situated at the minus end of the MT. The other domain is rich in tyr- tub
and extends from the plus end of the tyr-tub-poor domain to the end of the
MT. We have proposed that the spatial variation in the relative content of
tyr-tub along individual MTs reflects corresponding variations in their
dynamic properties. The present experiments have tested this hypothesis
directly by microinjecting biotin-labeled tubulin (Bt-tub) into cultured
sympathetic neurons and then quantifying the appearance of Bt-tub in the
tyr-tub-rich and tyr-tub-poor polymer of the axon. Bt-tub appeared in
axonal MTs with a half-life (t1/2) of approximately 2.2 hr. This time
course reflected an average of two distinct components corresponding to the
tyr-tub-rich and tyr-tub-poor polymer that had apparent t1/2 values of
approximately 1.3 and 3.3 hr, respectively. In individual MTs, Bt-tub first
appeared in the tyr-tub- rich domain and then only later appeared in the
tyr-tub-poor domain. Also, the appearance of Bt-tub in the tyr-tub-rich
polymer typically began precisely at its origin from the tyr-tub-poor
domain, indicating that the tyr-tub-poor polymer is assembly-competent and
nucleates the assembly of tyr-tub-rich polymer locally within the axon. The
stability properties of axonal MTs are discussed in terms of organizing MT
assembly locally in the axon and generating long MTs for growing long
axons.
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