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PMID:12374795

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Citation

Inman, GJ and Hill, CS (2002) Stoichiometry of active smad-transcription factor complexes on DNA. J. Biol. Chem. 277:51008-16

Abstract

Transforming growth factor (TGF)-beta signals through a heteromeric complex of serine/threonine kinase receptors. The type I receptor phosphorylates and activates the receptor-regulated Smads (R-Smads), Smad2 and Smad3, which form hetero-oligomeric complexes with the co-Smad, Smad4, and translocate to the nucleus. Smad3 and Smad4 can bind directly to consensus DNA-binding elements in the promoters of target genes, whereas Smad2/Smad4 complexes are targeted to DNA by interacting with sequence-specific DNA-binding transcription factors that contain a well-defined Smad interaction motif (SIM). The exact stoichiometry of Smad homo- and hetero-oligomers both before and after ligand stimulation is controversial. Here we determine the stoichiometry of TGF-beta-induced Smad-transcription factor complexes on DNA. We show that complexes of Smad2/Smad4 with the transcription factors Fast-1 or Fast-3 contain one Fast, two Smad2s, and one Smad4. In contrast, Smad3/Smad4 complexes that bind the Smad-binding element from the c-jun promoter, are heterodimers. Furthermore, these Smad3/Smad4 complexes contain at least two additional components essential for complex formation, one of which contains a SIM. Our data suggest that the R-Smads can form heterodimers or heterotrimers with Smad4, and we propose that the exact stoichiometries of active Smad complexes on DNA may be determined by the transcription factors with which they associate.

Links

PubMed Online version:10.1074/jbc.M208532200

Keywords

3T3 Cells; Animals; Base Sequence; Binding Sites; Cell Nucleus/metabolism; DNA Primers; Genes, jun; Humans; Kinetics; Mice; Mice, Knockout; Molecular Sequence Data; Plasmids/chemistry; Plasmids/metabolism; Polymerase Chain Reaction; Promoter Regions, Genetic; Smad4 Protein; Transcription Factors/chemistry; Transcription Factors/deficiency; Transcription Factors/genetics; Transcription Factors/metabolism; Transfection; Xenopus Proteins

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:SMAD4

part_of

GO:0005667: transcription regulator complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8JIT7

C

Seeded From UniProt

complete

HUMAN:SMAD4

part_of

GO:0005667: transcription regulator complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P70056

C

Seeded From UniProt

complete

XENLA:FAST3

part_of

GO:0032444: activin responsive factor complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13485

C

Seeded From UniProt

complete

XENLA:FAST3

part_of

GO:0032444: activin responsive factor complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q91912

C

Seeded From UniProt

complete

XENLA:Q91912

part_of

GO:0005667: transcription regulator complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8JIT7

C

Seeded From UniProt

complete

XENLA:Q91912

part_of

GO:0005667: transcription regulator complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P70056

C

Seeded From UniProt

complete

HUMAN:SMAD4

part_of

GO:0005667: transcription factor complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P70056

C

Seeded From UniProt

complete

HUMAN:SMAD4

part_of

GO:0005667: transcription factor complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q8JIT7

C

Seeded From UniProt

complete

XENLA:FOXH1

part_of

GO:0032444: activin responsive factor complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q91912

C

Seeded From UniProt

complete

XENLA:FOXH1

part_of

GO:0032444: activin responsive factor complex

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13485

C

Seeded From UniProt

complete


See also

References

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