부산대학교 도서관

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.bbrc.2006.10.083 Byline: Manda S. Krishnaveni (a), Jakob Lerche Hansen (b), Werner Seeger (a), Rory E. Morty (a), SA[cedilla]ren P. Sheikh (b), Oliver Eickelberg (a) Keywords: T[beta]RII-B; Extracellular domain; BRET; Receptor oligomerization; Signalling Abstract: Transforming growth factor (TGF)-[beta] ligands signal through transmembrane type I and type II serine/threonine kinase receptors, which form heteromeric signalling complexes upon ligand binding. Type II TGF-[beta] receptors (T[beta]RII) are reported to exist as homodimers at the cell surface, but the oligomerization pattern and dynamics of T[beta]RII splice variants in live cells has not been demonstrated thus far. Using co-immunoprecipitation and bioluminescence resonance energy transfer (BRET), we demonstrate that the mouse T[beta]RII receptor splice variant T[beta]RII-B is capable of forming ligand-independent homodimers and heterodimers with T[beta]RII. The homomeric interaction of mouse (m)T[beta]RII-B isoforms, however, is less robust than the heteromeric interactions of mT[beta]RII-B with wild-type T[beta]RII, which indicates that these receptors may be more likely to heterodimerize when both receptors are expressed. Moreover, we demonstrate that mT[beta]RII-B is a signalling receptor with ubiquitous tissue expression. Our study thus demonstrates previously unappreciated complex formation of TGF-[beta] type II receptors, and suggests that mT[beta]RII-B can direct TGF-[beta]-induced signalling in vitro and in vivo. Author Affiliation: (a) Department of Medicine II, University of Giessen Lung Center, Justus-Liebig University, Giessen, Germany (b) Laboratory of Molecular and Cellular Cardiology, The Heart Centre and The Danish National Research Foundation Centre for Cardiac Arrhythmia Copenhagen University Hospital, and the Faculty of Health, University of Copenhagen, Denmark Article History: Received 13 October 2006