Impact of NatC on N-terminal acetylome
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion Lumos
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Cell Culture
SUBMITTER: 
Annelies Bogaert
LAB HEAD: Kris Gevaert
PROVIDER: PXD034992 | Pride | 2023-09-13
REPOSITORIES: Pride
Dataset's files
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Publications
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity.
Varland Sylvia S Silva Rui Duarte RD Kjosås Ine I Faustino Alexandra A Bogaert Annelies A Billmann Maximilian M Boukhatmi Hadi H Kellen Barbara B Costanzo Michael M Drazic Adrian A Osberg Camilla C Chan Katherine K Zhang Xiang X Tong Amy Hin Yan AHY Andreazza Simonetta S Lee Juliette J JJ Nedyalkova Lyudmila L Ušaj Matej M Whitworth Alexander J AJ Andrews Brenda J BJ Moffat Jason J Myers Chad L CL Gevaert Kris K Boone Charles C Martinho Rui Gonçalo RG Arnesen Thomas T
Nature communications 20231027 1
Most eukaryotic proteins are N-terminally acetylated, but the functional impact on a global scale has remained obscure. Using genome-wide CRISPR knockout screens in human cells, we reveal a strong genetic dependency between a major N-terminal acetyltransferase and specific ubiquitin ligases. Biochemical analyses uncover that both the ubiquitin ligase complex UBR4-KCMF1 and the acetyltransferase NatC recognize proteins bearing an unacetylated N-terminal methionine followed by a hydrophobic residu ...[more]
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