Interaction and functional cooperation between the serine/threonine kinase bone morphogenetic protein type II receptor with the tyrosine kinase stem cell factor receptor
(2006) In Journal of Cellular Physiology 206(2). p.457-467- 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 rnorphogenetic 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... (More)
- 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 rnorphogenetic 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/421512
- author
- Hassel, Sylke ; Yakymovych, M ; Hellman, U ; Rönnstrand, Lars LU ; Knaus, P and Souchelnytskyi, S
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Cellular Physiology
- volume
- 206
- issue
- 2
- pages
- 457 - 467
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- pmid:16155937
- wos:000234458300022
- scopus:30344435306
- ISSN
- 1097-4652
- DOI
- 10.1002/jcp.20480
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
- id
- af20cbba-4750-428b-b7c4-59020995a213 (old id 421512)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16155937opt=Abstract
- date added to LUP
- 2016-04-01 12:11:44
- date last changed
- 2022-04-13 07:27:28
@article{af20cbba-4750-428b-b7c4-59020995a213, 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 rnorphogenetic 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.}}, author = {{Hassel, Sylke and Yakymovych, M and Hellman, U and Rönnstrand, Lars and Knaus, P and Souchelnytskyi, S}}, issn = {{1097-4652}}, language = {{eng}}, number = {{2}}, pages = {{457--467}}, publisher = {{John Wiley & Sons Inc.}}, series = {{Journal of Cellular Physiology}}, title = {{Interaction and functional cooperation between the serine/threonine kinase bone morphogenetic protein type II receptor with the tyrosine kinase stem cell factor receptor}}, url = {{http://dx.doi.org/10.1002/jcp.20480}}, doi = {{10.1002/jcp.20480}}, volume = {{206}}, year = {{2006}}, }