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PMID:8388127
Citation |
Ebner, R, Chen, RH, Shum, L, Lawler, S, Zioncheck, TF, Lee, A, Lopez, AR and Derynck, R (1993) Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor. Science 260:1344-8 |
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Abstract |
Transforming growth factor-beta (TGF-beta) affects cellular proliferation, differentiation, and interaction with the extracellular matrix primarily through interaction with the type I and type II TGF-beta receptors. The type II receptors for TGF-beta and activin contain putative serine-threonine kinase domains. A murine serine-threonine kinase receptor, Tsk 7L, was cloned that shared a conserved extracellular domain with the type II TGF-beta receptor. Overexpression of Tsk 7L alone did not increase cell surface binding of TGF-beta, but coexpression with the type II TGF-beta receptor caused TGF-beta to bind to Tsk 7L, which had the size of the type I TGF-beta receptor. Overexpression of Tsk 7L inhibited binding of TGF-beta to the type II receptor in a dominant negative fashion. Combinatorial interactions and stoichiometric ratios between the type I and II receptors may therefore determine the extent of TGF-beta binding and the resulting biological activities. |
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Keywords |
Amino Acid Sequence; Animals; Cell Line; Cercopithecus aethiops; Cloning, Molecular; Humans; Mice; Molecular Sequence Data; Protein-Serine-Threonine Kinases; Quail; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/genetics; Receptors, Cell Surface/metabolism; Receptors, Transforming Growth Factor beta; Transfection; Transforming Growth Factor beta/metabolism |
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Significance
Annotations
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