PARP1 ADP-ribosylates SMAD3 and SMAD4

Stable Identifier
R-HSA-2187325
Type
Reaction [transition]
Species
Homo sapiens
Compartment
nucleoplasm
ReviewStatus
5/5
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PARP1 ADP-ribosylates SMAD3 and SMAD4
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PARP1 ADP-ribosylates SMAD3 and SMAD4 in SMAD2/3:SMAD4 heterotrimer. ADP-ribosyl group is attached to glutamic acid residues E50 and E52 of SMAD3 and unknown amino acid residues of SMAD4. ADP-ribose monomer attached to SMAD3 and SMAD4 is subsequently extended to poly (ADP-ribosyl) chains (i.e. PAR chains) by PARP1, which is not shown here. ADP-ribosylation (PARylation) of SMAD3 and SMAD4 by PARP1 inhibits binding of SMAD2/3:SMAD4 heterotrimers to SMAD binding elements (SBEs) in promoters of SMAD-target genes.
Literature References
PubMed ID Title Journal Year
21095583 PARP-1 attenuates Smad-mediated transcription

Dahl, M, Lönn, P, Moustakas, A, Hellman, U, van der Heide, LP, Heldin, CH

Mol Cell 2010
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Catalyst Activity

NAD+-protein poly-ADP-ribosyltransferase activity of p-2S-SMAD2,3:SMAD4:PARP1 [nucleoplasm]

Physical Entity
p-2S-SMAD2,3:SMAD4:PARP1 [nucleoplasm] (Homo sapiens)
Activity
NAD+-protein poly-ADP-ribosyltransferase activity (GO:0003950)
Orthologous Events
PARP1 ADP-ribosylates SMAD3 and SMAD4 (Bos taurus)
PARP1 ADP-ribosylates SMAD3 and SMAD4 (Canis familiaris)
PARP1 ADP-ribosylates SMAD3 and SMAD4 (Drosophila melanogaster)
PARP1 ADP-ribosylates SMAD3 and SMAD4 (Mus musculus)
PARP1 ADP-ribosylates SMAD3 and SMAD4 (Rattus norvegicus)
PARP1 ADP-ribosylates SMAD3 and SMAD4 (Sus scrofa)
Authored
Orlic-Milacic, M  (2012-04-05)
Reviewed
Huang, T  (2012-05-14)
Contreras, O  (2022-05-02)
Created
Orlic-Milacic, M  (2012-04-09)
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