PuSH - Publikationsserver des Helmholtz Zentrums München: Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics.

Informationen

Hinweise zu Qualitätskriterien von Zeitschriften

Open-Access-Richtlinie der Helmholtz-Gemeinschaft 2016

CC Licencences

Metriken für Publikationen

Navigation

Startseite

English

EVA: Veröffentlichen

Neuer EVA Antrag

Recherche

Erweiterte Suche

Durchblättern nach ...

... HMGU-Autoren/Konsortien

... Organisationsstruktur

... Zeitschriften

... Publikationstypen

... Forschungsdaten

... Arbeitsgruppen

... Erscheinungsjahr

Publikationen im Überblick

Statistik

HGF Fortschrittsbericht

OA Publikationen

Eintragen

Neue Publikation eintragen

Neue Publikation holen aus...

...EVA

Fehlende Publikation melden

Highlights

Suche

Hilfe & Kontakt

Ansprechpartner

Hilfe

Datenschutz

Helmholtz Open Science

Bibliometrische Indikatoren

SHERPA/RoMEO

DOAJ

Export:

Text

Endnote (RIS) BIB

BibTeX

Vogl, A.M.* ; Phu, L.* ; Becerra, R.* ; Giusti, S.A.* ; Verschueren, E.* ; Hinkle, T.B.* ; Bordenave, M.D.* ; Adrian, M.* ; Heidersbach, A.* ; Yankilevich, P.* ; Stefani, F.D.* ; Wurst, W. ; Hoogenraad, C.C.* ; Kirkpatrick, D.S.* ; Refojo, D.* ; Sheng, M.*

Global site-specific neddylation profiling reveals that NEDDylated cofilin regulates actin dynamics.

Nat. Struct. Mol. Biol. 27, 210-220 (2020)

Verlagsversion

Forschungsdaten

DOI

PMC

Abstract
Metriken
Zusatzinfos

Neddylation is the post-translational protein modification most closely related to ubiquitination. Whereas the ubiquitin-like protein NEDD8 is well studied for its role in activating cullin−RING E3 ubiquitin ligases, little is known about other substrates. We developed serial NEDD8-ubiquitin substrate profiling (sNUSP), a method that employs NEDD8 R74K knock-in HEK293 cells, allowing discrimination of endogenous NEDD8- and ubiquitin-modification sites by MS after Lys-C digestion and K-εGG-peptide enrichment. Using sNUSP, we identified 607 neddylation sites dynamically regulated by the neddylation inhibitor MLN4924 and the de-neddylating enzyme NEDP1, implying that many non-cullin proteins are neddylated. Among the candidates, we characterized lysine 112 of the actin regulator cofilin as a novel neddylation event. Global inhibition of neddylation in developing neurons leads to cytoskeletal defects, altered actin dynamics and neurite growth impairments, whereas site-specific neddylation of cofilin at K112 regulates neurite outgrowth, suggesting that cofilin neddylation contributes to the regulation of neuronal actin organization.

Impact Factor

Scopus SNIP

Scopus
Cited By

Altmetric

11.980

2.237