FICD activity and AMPylation remodelling modulate human neurogenesis
Open accessPublished version of a preprint
Abstract
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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Self-citation
- Authors
- Kielkowski, P., Buchsbaum, I. Y., Kirsch, V. C., Bach, N. C., Drukker, M., Cappello, S., & Sieber, S. A.
- Affiliations
- Technical University of Munich (DE)
- Max Planck Institute of Psychiatry (DE)
- Helmholtz Munich (DE)
- Corresponding author
- Cappello, Silvia
- Sieber, Stephan A.
- ORCID
- Venue
- Nature Communications
- Published
- 2020-01-24
- Volume
- 11
- Issue
- 1
- Pages
- 517-517
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC6981130
- OpenAlex
- W3001174176
- Cited by
- 65
- References
- 7
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 8 · 2023: 3 · 2022: 14 · 2021: 12 · 2020: 12
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Leiden Repository (Leiden University) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- mediaTUM (Technical University of Munich) (submittedVersion, other-oa)
- Leiden Repository (Leiden University) (submittedVersion)
- Site cant be reached (submittedVersion, cc-by)
- MPG.PuRe (Max Planck Society) (submittedVersion, cc-by)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion, cc-by)
- Data Archiving and Networked Services (DANS) (submittedVersion, cc-by)
- Funders
- H2020 European Research Council (725085)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- AMPylation, adenylylation, post-translational modification, neural progenitor cells, brain organoids, neuronal differentiation
- MeSH terms
- Adenosine, Adenosine Monophosphate, Amino Acid Sequence, Cathepsin B, Cell Differentiation, Humans, Membrane Proteins, Neurons, Nucleotidyltransferases, Organoids, Protein Processing, Post-Translational, Down-Regulation, Cell Line, Tumor, Neurogenesis, Neural Stem Cells
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