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Acetylated α-tubulin K394 regulates microtubule stability to shape the growth of axon terminals.
Saunders, Harriet A J; Johnson-Schlitz, Dena M; Jenkins, Brian V; Volkert, Peter J; Yang, Sihui Z; Wildonger, Jill.
Afiliación
  • Saunders HAJ; Integrated Program in Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
  • Johnson-Schlitz DM; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
  • Jenkins BV; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
  • Volkert PJ; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA; Biochemistry Scholars Program, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA.
  • Yang SZ; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA; Cellular & Molecular Biology Graduate Program, University of Wisconsin-Madison, 1525 Linden Drive, Madison, WI 53706, USA.
  • Wildonger J; Department of Biochemistry, University of Wisconsin-Madison, 440 Henry Mall, Madison, WI 53706, USA. Electronic address: jwildonger@health.ucsd.edu.
Curr Biol ; 32(3): 614-630.e5, 2022 02 07.
Article en En | MEDLINE | ID: mdl-35081332
Microtubules are essential to neuron shape and function. Acetylation of tubulin has the potential to directly tune the behavior and function of microtubules in cells. Although proteomic studies have identified several acetylation sites in α-tubulin, the effects of acetylation at these sites remains largely unknown. This includes the highly conserved residue lysine 394 (K394), which is located at the αß-tubulin dimer interface. Using a fly model, we show that α-tubulin K394 is acetylated in the nervous system and is an essential residue. We found that an acetylation-blocking mutation in endogenous α-tubulin, K394R, perturbs the synaptic morphogenesis of motoneurons and reduces microtubule stability. Intriguingly, the K394R mutation has opposite effects on the growth of two functionally and morphologically distinct motoneurons, revealing neuron-type-specific responses when microtubule stability is altered. Eliminating the deacetylase HDAC6 increases K394 acetylation, and the over-expression of HDAC6 reduces microtubule stability similar to the K394R mutant. Thus, our findings implicate α-tubulin K394 and its acetylation in the regulation of microtubule stability and suggest that HDAC6 regulates K394 acetylation during synaptic morphogenesis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tubulina (Proteína) / Terminales Presinápticos Tipo de estudio: Prognostic_studies Idioma: En Revista: Curr Biol Asunto de la revista: BIOLOGIA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tubulina (Proteína) / Terminales Presinápticos Tipo de estudio: Prognostic_studies Idioma: En Revista: Curr Biol Asunto de la revista: BIOLOGIA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido