N‐terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects

The vast majority of eukaryotic proteins are N‐terminally modified by one or more processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include different peptidases, transferases, and ligases. Methionine aminopeptidases excise the initiator methionine leaving the nascent polypeptide with a newly exposed amino acid that may be further modified. N‐terminal acetyl‐, methyl‐, myristoyl‐, and palmitoyltransferases may attach an acetyl, methyl, myristoyl, or palmitoyl group, respectively, to the α‐amino group of the target protein N‐terminus. With the action of ubiquitin ligases, one or several ubiquitin molecules are transferred, and hence, constitute the N‐terminal modification. Modifications at protein N‐termini represent an important contribution to proteomic diversity and complexity, and are essential for protein regulation and cellular signaling. Consequently, dysregulation of the N‐terminal modifying enzymes is implicated in human diseases. We here review the different protein N‐terminal modifications occurring co‐ or post‐translationally with emphasis on the responsible enzymes and their substrate specificities.

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch

Erschienen in
N‐terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effects ; volume:15 ; number:14 ; year:2015 ; pages:2385-2401 ; extent:17
Proteomics ; 15, Heft 14 (2015), 2385-2401 (gesamt 17)

Urheber
Varland, Sylvia
Osberg, Camilla
Arnesen, Thomas

DOI
10.1002/pmic.201400619
URN
urn:nbn:de:101:1-2022112407311473434778
Rechteinformation
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Letzte Aktualisierung
15.08.2025, 07:21 MESZ

Datenpartner

Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.

Beteiligte

  • Varland, Sylvia
  • Osberg, Camilla
  • Arnesen, Thomas

Ähnliche Objekte (12)