Details

Autor(en) / Beteiligte

• Song, Yuyu
• Kirkpatrick, Laura L.
• Schilling, Alexander B.
• Helseth, Donald L.
• Chabot, Nicolas
• Keillor, Jeffrey W.
• Johnson, Gail V.W.
• Brady, Scott T.

Titel

Transglutaminase and Polyamination of Tubulin: Posttranslational Modification for Stabilizing Axonal Microtubules

Ist Teil von

• Neuron (Cambridge, Mass.), 2013-04, Vol.78 (1), p.109-123

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2013

Link zum Volltext

Quelle

Electronic Journals Library

Beschreibungen/Notizen

• Neuronal microtubules support intracellular transport, facilitate axon growth, and form a basis for neuronal morphology. While microtubules in nonneuronal cells are depolymerized by cold, Ca2+, or antimitotic drugs, neuronal microtubules are unusually stable. Such stability is important for normal axon growth and maintenance, while hyperstability may compromise neuronal function in aging and degeneration. Though mechanisms for stability are unclear, studies suggest that stable microtubules contain biochemically distinct tubulins that are more basic than conventional tubulins. Transglutaminase-catalyzed posttranslational incorporation of polyamines is one of the few modifications of intracellular proteins that add positive charges. Here we show that neuronal tubulin can be polyaminated by transglutaminase. Endogenous brain transglutaminase-catalyzed polyaminated tubulins have the biochemical characteristics of neuronal stable microtubules. Inhibiting polyamine synthesis or transglutaminase activity significantly decreases microtubule stability in vitro and in vivo. Together, these findings suggest that transglutaminase-catalyzed polyamination of tubulins stabilizes microtubules essential for unique neuronal structures and functions. ► A novel modification of neuronal tubulin involves polyamination by transglutaminase ► Tubulin polyamination stabilizes microtubules and is enriched in axonal domains ► Transglutaminase-catalyzed polyamination of tubulin is developmentally regulated ► Tubulin polyamination may be essential for neurite outgrowth and axon maturation Song et al. expand the repertoire of tubulin posttranslational modifications by discovering that neuronal tubulin can be polyaminated by transglutaminase. Tubulin polyamination stabilizes axonal microtubules and may contribute to the regulation of neurite differentiation and maturation of axonal connections.