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- Title
Interaction and functional cooperation between the serine/threonine kinase bone morphogenetic protein type II receptor with the tyrosine kinase stem cell factor receptor<FNR></FNR><FN>This article includes Supplementary Material available from the authors upon request or via the Internet at <URL>http://www.interscience.wiley.com/jpages/0021-9541/suppmat</URL>. </FN>
- Authors
Hassel, Sylke; Yakymovych, Mariya; Hellman, Ulf; Rönnstrand, Lars; Knaus, Petra; Souchelnytskyi, Serhiy
- Abstract
Transmembrane receptors with intrinsic serine/threonine or tyrosine kinase domains regulate vital functions of cells in multicellular eukaryotes, e.g., differentiation, apoptosis, and proliferation. Here, we show that bone morphogenetic protein type II receptor (BMPR-II) which has a serine/threonine kinase domain, and stem cell factor receptor (c-kit) which contains a tyrosine kinase domain form a complex in vitro and in vivo; the interaction is induced upon treatment of cells with BMP2 and SCF. Stem cell factor (SCF) modulated BMP2-dependent activation of Smad1/5/8 and phosphorylation of Erk kinase. SCF also enhanced BMP2-dependent differentiation of C2C12 cells. We found that BMPR-II was phosphorylated at Ser757 upon co-expression with and activation of c-kit. BMPR-II phosphorylation required intact kinase activity of BMPR-II. Abrogation of the c-kit/SCF-dependent phosphorylation of BMPR-II at the Ser757 interfered with the cooperative effect of BMP2 and SCF. Our data suggest that the complex formation between c-kit and BMPR-II leads to phosphorylation of BMPR-II at Ser757, which modulates BMPR-II-dependent signaling. J. Cell. Physiol. 206: 457–467, 2006. © 2005 Wiley-Liss, Inc.
- Subjects
SERINE; PROTEIN-tyrosine kinases; APOPTOSIS; BONE morphogenetic proteins; PHOSPHORYLATION; STEM cells
- Publication
Journal of Cellular Physiology, 2006, Vol 206, Issue 2, p457
- ISSN
0021-9541
- Publication type
Article
- DOI
10.1002/jcp.20480