Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 277, Issue 34, Pages 30690-30698Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M204930200
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Funding
- NCI NIH HHS [T32 CA 09503] Funding Source: Medline
- NIGMS NIH HHS [T32 GM 08224] Funding Source: Medline
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Detyrosination is an evolutionarily conserved post-translational modification of microtubule polymers that is known to be enhanced during early morphological differentiation of cultured myogenic cells (Gundersen, G. G., Khawaja, S., and Bulinski, J. C. (1989) J. Cell Biol. 109, 2275-2288). We proposed that altering the C terminus of a-tubulin by detyrosination plays a role in morphological differentiation. To test our hypothesis, we treated L6 myoblasts with 3-nitrotyrosine (Eiserich, J. P., Estevez, A. G., Bamberg, T. V., Ye, Y. Z., Chuniley, P. H., Beckman, J. S., and Freeman, B. A. (1999) Proc. Natl. Acad. Sci. U. S. A. 96,6365-6375), a nontoxic inhibitor that resulted in high level inhibition of microtubule detyrosination and low level incorporation of nitrotyrosine into microtubules. Even though microtubule stabilization or modification by acetylation still occurred normally, morphological differentiation was blocked; myoblasts neither elongated significantly nor fused. Nitrotyrosine treatment prevented synthesis or activation of markers of myogenic differentiation, including muscle-specific myosin, alpha-actin, integrin alpha(7), and myogenin. Consistent with this, myoblast integrin beta(1A) remained highly expressed. In contrast, the increase in beta-catenin level characteristic of early myogenesis was unaffected by treatment. These results show that the identity of the C-terminal residue of alpha-tubulin modulates microtubule activity, possibly because binding to or signaling from modified microtubules is required for the myogenic program.
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