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PMID:7852346

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Citation

Lin, HY, Moustakas, A, Knaus, P, Wells, RG, Henis, YI and Lodish, HF (1995) The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. J. Biol. Chem. 270:2747-54

Abstract

The transforming growth factor (TGF)-beta type II receptor is a transmembrane serine/threonine kinase which is essential for all TGF-beta-induced signals. In several cell types TGF-beta 2 is as potent as TGF-beta or TGF-beta 3 in inducing cellular responses, yet TGF-beta 2 does not bind to the majority of expressed type II receptors. Here we characterized the properties of the soluble extracellular domain of the human TGF-beta type II receptor synthesized in COS-7 cells. Like the membrane-attached type II receptor, the soluble receptor contains complex N-linked oligosaccharides as well as additional sialic acid residues that cause it to migrate heterogenously upon SDS-polyacrylamide gel electrophoresis. 125I-TGF-beta 1 binds to and is chemically cross-linked to this protein. Unlabeled TGF-beta 1 inhibits the binding of 125I-TGF-beta 1 with an apparent dissociation constant (Kd) of approximately 200 pM, similar to the apparent Kd (approximately 50 pM) of the cell-surface type II receptor. TGF-beta 3 inhibits the binding of 125I-TGF-beta 1 to the soluble type II receptor with a similar dissociation constant, approximately 500 pM. In contrast, 125I-TGF-beta 2 cannot bind and be chemically cross-linked to the soluble type II receptor, nor does as much as a 125-fold excess of unlabeled TGF-beta 2 inhibit the binding of 125I-TGF-beta 1 to the soluble receptor. This is the first demonstration of the binding affinities of the type II receptor in the absence of the other cell-surface molecules known to bind TGF-beta. Expressed alone in COS-7 cells the type II receptor also cannot bind TGF-beta 2; co-expression of type III receptor enables the type II receptor to bind TGF-beta 2. Thus, the type III receptor or some other component is required for transmission of TGF-beta 2-induced signals by the type II receptor.

Links

PubMed

Keywords

Animals; Base Sequence; Cell Line; Cross-Linking Reagents; Glycosylation; Humans; Iodine Radioisotopes; Ligands; Molecular Sequence Data; Protein Binding; Receptors, Transforming Growth Factor beta/metabolism; Transforming Growth Factor beta/metabolism

Significance

Annotations

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

HUMAN:TGFB1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P37173

F

Seeded From UniProt

complete

HUMAN:TGFB3

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P37173

F

Seeded From UniProt

complete

RAT:TGBR3

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P61812

F

Seeded From UniProt

complete

RAT:TGBR3

part_of

GO:0043235: receptor complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

RAT:TGBR3

contributes_to

GO:0050431: transforming growth factor beta binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P61812

F

Seeded From UniProt

complete

HUMAN:TGFR2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P10600

F

Seeded From UniProt

complete

HUMAN:TGFR2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P01137

F

Seeded From UniProt

complete

HUMAN:TGFR2

located_in

GO:0016021: integral component of membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:TGFB2

enables

GO:0034714: type III transforming growth factor beta receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P26342

F

Seeded From UniProt

complete

HUMAN:TGFB2

enables

GO:0005114: type II transforming growth factor beta receptor binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P37173

F

Seeded From UniProt

complete

HUMAN:TGFR2

enables

GO:0050431: transforming growth factor beta binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:TGFR2

part_of

GO:0043235: receptor complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:TGFR2

enables

GO:0005539: glycosaminoglycan binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:TGFR2

contributes_to

GO:0050431: transforming growth factor beta binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P61812

F

Seeded From UniProt

complete

HUMAN:TGFR2

part_of

GO:0016021: integral component of membrane

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:TGFR2

enables

GO:0005024: transforming growth factor beta-activated receptor activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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