Your browser doesn't support javascript.
loading
The role of protein acetylation in regulating mitochondrial fusion and fission.
Uddin, Golam M; Abbas, Rafa; Shutt, Timothy E.
Afiliação
  • Uddin GM; Departments of Medical Genetics and Biochemistry and Molecular Biology, Alberta Children's Hospital Research Institute, Hotchkiss Brain Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
  • Abbas R; Departments of Medical Genetics and Biochemistry and Molecular Biology, Alberta Children's Hospital Research Institute, Hotchkiss Brain Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
  • Shutt TE; Departments of Medical Genetics and Biochemistry and Molecular Biology, Alberta Children's Hospital Research Institute, Hotchkiss Brain Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
Biochem Soc Trans ; 49(6): 2807-2819, 2021 12 17.
Article em En | MEDLINE | ID: mdl-34812890
ABSTRACT
The dynamic processes of mitochondrial fusion and fission determine the shape of mitochondria, which can range from individual fragments to a hyperfused network, and influence mitochondrial function. Changes in mitochondrial shape can occur rapidly, allowing mitochondria to adapt to specific cues and changing cellular demands. Here, we will review what is known about how key proteins required for mitochondrial fusion and fission are regulated by their acetylation status, with acetylation promoting fission and deacetylation enhancing fusion. In particular, we will examine the roles of NAD+ dependant sirtuin deacetylases, which mediate mitochondrial acetylation, and how this post-translational modification provides an exquisite regulatory mechanism to co-ordinate mitochondrial function with metabolic demands of the cell.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas / Dinâmica Mitocondrial / Mitocôndrias Idioma: En Revista: Biochem Soc Trans Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Canadá

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas / Dinâmica Mitocondrial / Mitocôndrias Idioma: En Revista: Biochem Soc Trans Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Canadá