Interaction of Transforming Growth Factor β Receptors with Apolipoprotein J/Clusterin

Proteins mediating the transmission of the signal from an activated transforming growth factor β (TGFβ) receptor complex have not been identified. Using a yeast interaction screen to search for proteins that associate with the type II TGFβ receptor (RII), we isolated a protein which was identical to...

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Bibliographic Details
Published in:Biochemistry (Easton) 1996-01, Vol.35 (1), p.309-314
Main Authors: Reddy, Kumar B, Karode, Mary C, Harmony, Judith A. K, Howe, Philip H
Format: Article
Language:English
Subjects:
Base Sequence
Binding Sites
Brain - metabolism
Cloning, Molecular
Clusterin
DNA Primers
DNA, Complementary
Female
Gene Library
Glycoproteins - chemistry
Glycoproteins - metabolism
Humans
Molecular Chaperones
Molecular Sequence Data
Placenta - metabolism
Pregnancy
Receptor, Epidermal Growth Factor - metabolism
Receptors, Transforming Growth Factor beta - chemistry
Receptors, Transforming Growth Factor beta - metabolism
Recombinant Fusion Proteins - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Saccharomyces cerevisiae - growth & development
Sequence Deletion
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Summary:Proteins mediating the transmission of the signal from an activated transforming growth factor β (TGFβ) receptor complex have not been identified. Using a yeast interaction screen to search for proteins that associate with the type II TGFβ receptor (RII), we isolated a protein which was identical to apolipoprotein J (apoJ)/clusterin. ApoJ interacts with both the type I (RI) and type II (RII) TGFβ receptors but does not interact with the epidermal growth factor (EGF) receptor. The interaction between RII and apoJ occurs through the C-terminal 127 amino acids of RII. Deletion of this region, which contains the kinase insert 2 domain, abrogates binding to apoJ. The binding of apoJ to either the RI and the RII receptors is direct, not requiring other proteins, and is not specific for the α or β subunit of apoJ since both subunits are effective in competing for binding. RI and RII fusion proteins are capable of precipitating the 60 kDa intracellular form of apoJ from [35S]methionine-labeled cellular lysates, suggesting that this form of the protein may play some role in TGFβ signaling or TGFβ receptor processing.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi951880a