Promotion of microtubule assembly by neurofilament-associated microtubule-associated proteins.

Abstract:

:Intact neurofilaments (NF) purified from mammalian brain and spinal cord promote the assembly of microtubules in solutions of pure phosphocellulose (PC)-purified tubulin. This assembly is temperature-dependent and is inhibited by mitotic spindle inhibitors. The ability of NF to induce microtubule formation is 20% of that of purified microtubule-associated proteins (MAPs), whereas MAPs comprise less than 5% of the protein in the NF preparations. The inducing activity of NF is rapidly lost on boiling. When intact NF are incubated with PC-tubulin and then centrifuged, tubulin is sedimented together with the filaments. This association is inhibited by colchicine and podophyllotoxin and is cold-sensitive. NF purified to homogeneity under denaturing conditions and then reassembled completely lack the ability to promote the assembly of PC-tubulin or to bind tubulin on a centrifugation assay. No MAPs are present in these preparations, though these filaments have the ability to bind exogenous MAPs. While these experiments do not rule out an intrinsic microtubule-assembly-promoting activity, they suggest that this activity is due to nontriplet proteins in the preparation, most likely filament-associated MAPs.

journal_name

J Neurochem

authors

Leterrier JF,Wong J,Liem RK,Shelanski ML

doi

10.1111/j.1471-4159.1984.tb05398.x

subject

Has Abstract

pub_date

1984-11-01 00:00:00

pages

1385-91

issue

5

eissn

0022-3042

issn

1471-4159

journal_volume

43

pub_type

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