Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors

Experimental Cell Research
J P de WinterA J Van Den Eijden-Van Raaij

Abstract

Truncated activin type II receptors have been reported to inhibit activin receptor signaling in Xenopus embryos, although the mechanism of action for this effect has not been fully understood. In the present study we demonstrate that in P19 embryonal carcinoma cells both the induction of the activin responsive 3TP-lux reporter construct and the inhibition of retinoic acid-induced neuronal differentiation by activin are blocked by expression of a truncated activin receptor. To reveal the mechanism of action of truncated activin receptors, the interaction between different activin receptors has been investigated upon coexpression in COS cells followed by cross-linking of 125I-activin A and subsequent immunoprecipitation. Complexes between a truncated activin type IIA receptor and activin type IA and type IB receptors can be formed, as demonstrated by coimmunoprecipitation of these type I receptors with the truncated activin type IIA receptor. Other type I receptors known as ALK-1 and ALK-6 also coimmunoprecipitate with the truncated type IIA receptor, whereas ALK-3 and ALK-5 do not. Furthermore, the activin type IIB2 receptor does not coimmunoprecipitate with the truncated type IIA receptor, but decreases activin binding to the t...Continue Reading

Citations

Aug 1, 1997·Developmental Dynamics : an Official Publication of the American Association of Anatomists·B A RoelenC L Mummery
Jul 31, 2018·Human Molecular Genetics·Dandi QiaoMichael H Cho
Jun 1, 1997·Current Opinion in Genetics & Development·N Josso, N di Clemente
May 30, 1998·Biochemical Pharmacology·T K Woodruff
Mar 7, 2000·The American Journal of Pathology·B S Jacobson

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