The role of Nα-terminal acetylation in protein conformation.

N‐terminal acetylation N‐terminal acetyltransferases actin alpha‐synuclein fused in Sarcoma huntingtin parvalbumin protein folding proteomics tropomyosin

Journal

The FEBS journal

ISSN: 1742-4658

Titre abrégé: FEBS J

Pays: England

ID NLM: 101229646

Informations de publication

Date de publication:
23 Jun 2024

Historique:

received: 28 03 2024

accepted: 12 06 2024

medline: 26 6 2024

pubmed: 26 6 2024

entrez: 26 6 2024

Statut: aheadofprint

Résumé

Especially in higher eukaryotes, the N termini of proteins are subject to enzymatic modifications, with the acetylation of the alpha-amino group of nascent polypeptides being a prominent one. In recent years, the specificities and substrates of the enzymes responsible for this modification, the Nα-terminal acetyltransferases, have been mapped in several proteomic studies. Aberrant expression of, and mutations in these enzymes were found to be associated with several human diseases, explaining the growing interest in protein Nα-terminal acetylation. With some enzymes, such as the Nα-terminal acetyltransferase A complex having thousands of possible substrates, researchers are now trying to decipher the functional outcome of Nα-terminal protein acetylation. In this review, we zoom in on one possible functional consequence of Nα-terminal protein acetylation; its effect on protein folding. Using selected examples of proteins associated with human diseases such as alpha-synuclein and huntingtin, here, we discuss the sometimes contradictory findings of the effects of Nα-terminal protein acetylation on protein (mis)folding and aggregation.

Identifiants

DOI: 10.1111/febs.17209 PMID: 38923676

pubmed: 38923676

doi: 10.1111/febs.17209

doi:

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

Subventions

Organisme : Fonds Wetenschappelijk Onderzoek

ID : G002721N

Informations de copyright

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