Abstract：
:We have examined the question of whether alpha-tubulin is detyrosylated during axonal transport in retinal ganglion cell axons and axons of spinal motor neurons. The degree of tyrosylation of alpha-tubulin was estimated from immunocytochemistry and immunoblotting with two anti-alpha-tubulin monoclonals, one of which (YL1/2) recognizes only the tyrosylated form of alpha-tubulin. In the case of retinal ganglion cells, the axons were depleted of tyrosylated alpha-tubulin both in the retina and proximal region of the optic nerve. Distal regions of the axons, in the optic tract, gave a pattern of staining consistent with a reduction in the total level of alpha-tubulin at the expense of detyrosylated alpha-tubulin. Axons within the L5 ventral root, the sciatic nerve and tibial nerve were consistently unstained by YL1/2 indicating that these axons were depleted in tyrosylated alpha-tubulin in all 3 segments. The results indicate that alpha-tubulin destined for axonal microtubules is detyrosylated close to or in cell bodies and not progressively during its transport. Therefore the segregation of detyrosylated alpha-tubulin to axonal microtubules may occur at their site of assembly.
journal_name
Brain Resjournal_title
Brain researchauthors
Burgoyne RD,Norman KMdoi
10.1016/0006-8993(86)90697-9subject
Has Abstractpub_date
1986-08-27 00:00:00pages
113-20issue
1eissn
0006-8993issn
1872-6240pii
0006-8993(86)90697-9journal_volume
381pub_type
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