Overlap of NatA and IAP substrates implicates N-terminal acetylation in protein stabilization-Reference-Cited by-同舟云学术

Overlap of NatA and IAP substrates implicates N-terminal acetylation in protein stabilization

Published:2021-01-15 Issue:3 Volume:7 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Mueller Franziska¹^ORCID,Friese Alexandra¹,Pathe Claudio¹^ORCID,da Silva Richard Cardoso¹^ORCID,Rodriguez Kenny Bravo¹,Musacchio Andrea¹²^ORCID,Bange Tanja¹³^ORCID

Affiliation:

1. Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227 Dortmund, Germany.

2. Centre for Medical Biotechnology, Faculty of Biology, University Duisburg-Essen, Universitaetsstrasse, 45141 Essen, Germany.

3. Institute of Medical Psychology, Faculty of Medicine, LMU Munich.

Abstract

N-terminal acetylation by NATA acetyltransferase shields many of its targets from inhibitor of apoptosis ubiquitin ligases.

Funder

European Research Council

Deutsche Forschungsgemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference74 articles.

1. Protein N-Terminal Processing: Substrate Specificity of Escherichia coli and Human Methionine Aminopeptidases

2. Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases

3. N-terminal Acetylation Levels Are Maintained During Acetyl-CoA Deficiency in Saccharomyces cerevisiae

4. Metabolic Regulation of Protein N-Alpha-Acetylation by Bcl-xL Promotes Cell Survival

5. Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown.

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