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Kielkowski, P.* ; Buchsbaum, I.Y.* ; Kirsch, V.C.* ; Bach, N.C.* ; Drukker, M. ; Cappello, S.* ; Sieber, S.A.*

FICD activity and AMPylation remodelling modulate human neurogenesis.

Nat. Commun. 11:517 (2020)
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Open Access Gold
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Posttranslational modification (PTM) of proteins represents an important cellular mechanism for controlling diverse functions such as signalling, localisation or protein-protein interactions. AMPylation (also termed adenylylation) has recently been discovered as a prevalent PTM for regulating protein activity. In human cells AMPylation has been exclusively studied with the FICD protein. Here we investigate the role of AMPylation in human neurogenesis by introducing a cell-permeable propargyl adenosine pronucleotide probe to infiltrate cellular AMPylation pathways and report distinct modifications in intact cancer cell lines, human-derived stem cells, neural progenitor cells (NPCs), neurons and cerebral organoids (COs) via LC-MS/MS as well as imaging methods. A total of 162 AMP modified proteins were identified. FICD-dependent AMPylation remodelling accelerates differentiation of neural progenitor cells into mature neurons in COs, demonstrating a so far unknown trigger of human neurogenesis.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Posttranslational Modifications; Endoplasmic-reticulum; Protein; Mechanism; Proteomics; Diversity; Discovery; Reveals; Gtpases; Enzyme
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Quellenangaben Volume: 11, Issue: 1, Pages: , Article Number: 517 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed