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Journal article

Suppression of TGF-β/SMAD signaling by an inner nuclear membrane phosphatase complex

Abstract:
Cytokines of the TGF-β superfamily control essential cell fate decisions via receptor regulated SMAD (R-SMAD) transcription factors. Ligand-induced R-SMAD phosphorylation in the cytosol triggers their activation and nuclear accumulation. We determine how R-SMADs are inactivated by dephosphorylation in the cell nucleus to counteract signaling by TGF-β superfamily ligands. We show that R-SMAD dephosphorylation is mediated by an inner nuclear membrane associated complex containing the scaffold protein MAN1 and the CTDNEP1-NEP1R1 phosphatase. Structural prediction, domain mapping and mutagenesis reveals that MAN1 binds independently to the CTDNEP1-NEP1R1 phosphatase and R-SMADs to promote their inactivation by dephosphorylation. Disruption of this complex causes nuclear accumulation of R-SMADs and aberrant signaling, even in the absence of TGF-β ligands. These findings establish CTDNEP1-NEP1R1 as the R-SMAD phosphatase, reveal the mechanistic basis for TGF-β signaling inactivation and highlight how this process is disrupted by disease-associated MAN1 mutations.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-025-58681-x

Authors

More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
ORCID:
0009-0008-8847-1910
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
ORCID:
0009-0008-8176-7161


More from this funder
Funder identifier:
https://ror.org/029chgv08
Funding agency for:
Carvalho, P
Trost, M
Grant:
223153/Z/21/Z
215542/Z/19/Z
212947/Z/18/Z
More from this funder
Funder identifier:
https://ror.org/0472cxd90
Funding agency for:
Carvalho, P
Grant:
817708


Publisher:
Nature Research
Journal:
Nature Communications More from this journal
Volume:
16
Issue:
1
Article number:
3474
Publication date:
2025-04-11
Acceptance date:
2025-03-28
DOI:
EISSN:
2041-1723


Language:
English
Pubs id:
2106288
Local pid:
pubs:2106288
Deposit date:
2025-04-07
ARK identifier:

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