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. 2000 May 1;149(3):667–682. doi: 10.1083/jcb.149.3.667

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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Expression of cytoplasmically truncated dnTβRII in stably infected preadipocytes (A) and adipocytes (B). Cell-surface availability of TGF-β receptors was assessed by binding and chemical cross-linking to [¹²⁵I]TGF-β. The first two lanes of each panel contain samples of total lysates, whereas the last two lanes contain immunoprecipitations using anti-Flag antibody, which recognizes the Flag epitope tag of dnTβRII. Positions of TβRII (RII), TβRI (RI), and dnTβRII are indicated. Endogenous TβRI coprecipitated with the dnTβRII, as expected. The mobility of the receptors was slightly different in total lysates versus immunoprecipitates because of differing salt conditions and/or the presence of IgG in the immunoprecipitates. Exposure times were identical for all panels.