Journal
CELL REPORTS
Volume 10, Issue 8, Pages 1362-1374Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2015.01.053
Keywords
-
Categories
Funding
- Norwegian Cancer Society
- Bergen Research Foundation BFS
- Research Council of Norway [197136, 230865]
- Western Norway Regional Health Authority
- Research Foundation - Flanders (FWO-Vlaanderen) [G.0269.13N]
Ask authors/readers for more resources
N-terminal acetylation is a major and vital protein modification catalyzed by N-terminal acetyltransferases (NATs). NatF, or N alpha-acetyltransferase 60 (Naa60), was recently identified as a NAT in multicellular eukaryotes. Here, we find that Naa60 differs from all other known NATs by its Golgi localization. A new membrane topology assay named PROMPT and a selective membrane permeabilization assay established that Naa60 faces the cytosolic side of intracellular membranes. An Nt-acetylome analysis of NAA60-knockdown cells revealed that Naa60, as opposed to other NATs, specifically acetylates transmembrane proteins and has a preference for N termini facing the cytosol. Moreover, NAA60 knockdown causes Golgi fragmentation, indicating an important role in the maintenance of the Golgi's structural integrity. This work identifies a NAT associated with membranous compartments and establishes N-terminal acetylation as a common modification among transmembrane proteins, a thus-far poorly characterized part of the N-terminal acetylome.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available