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N-terminal acetylation of actin by NAA80 is essential for structural integrity of the Golgi apparatus.

Exp Cell Res. 2020 May 15;390(2):111961. Epub 2020 Mar 21
Tobias B Beigl 1 , Monica Hellesvik 2 , Jaakko Saraste 2 , Thomas Arnesen 3 , Henriette Aksnes 4
Tobias B Beigl 1 , Monica Hellesvik 2 , Jaakko Saraste 2 , Thomas Arnesen 3 , Henriette Aksnes 4

[No authors listed]

Author information
  • 1 Department of Biomedicine, University of Bergen, Norway; Institute of Cell Biology and Immunology, University of Stuttgart, Germany.
  • 2 Department of Biomedicine, University of Bergen, Norway.
  • 3 Department of Biomedicine, University of Bergen, Norway; Department of Biological Sciences, University of Bergen, Norway; Department of Surgery, Haukeland University Hospital, Norway.
  • 4 Department of Biomedicine, University of Bergen, Norway. Electronic address: henriette.aksnes@uib.no.

摘要


N-alpha-acetyltransferase 80 (NAA80) was recently demonstrated to acetylate the N-terminus of actin, with NAA80 knockout cells showing actin cytoskeleton-related phenotypes, such as increased formation of membrane protrusions and accelerated migration. Here we report that NAA80 knockout cells additionally display fragmentation of the Golgi apparatus. We further employed rescue assays to demonstrate that this phenotype is connected to the ability of NAA80 to modify actin. Thus, re-expression of NAA80, which leads to re-establishment of actin's N-terminal acetyl group, rescued the Golgi fragmentation, whereas a catalytic dead NAA80 mutant could neither restore actin Nt-acetylation nor Golgi structure. The Golgi phenotype of NAA80 KO cells was shared by both migrating and non-migrating cells and live-cell imaging indicated increased Golgi dynamics in migrating NAA80 KO cells. Finally, we detected a drastic increase in the amount of F-actin in cells lacking NAA80, suggesting a causal relationship between this effect and the observed re-organization of Golgi structure. The findings further underscore the importance of actin Nt-acetylation and provide novel insight into its cellular roles, suggesting a mechanistic link between actin modification state and Golgi organization.

KEYWORDS: Actin cytoskeleton, Cell migration, Golgi structure, N-alpha-acetyltransferase 80 (NAA80), N-terminal acetylation, Posttranslational modification