» Articles » PMID: 22961979

SMAD Versus Non-SMAD Signaling is Determined by Lateral Mobility of Bone Morphogenetic Protein (BMP) Receptors

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2012 Sep 11
PMID 22961979
Citations 32
Authors
Affiliations
Soon will be listed here.
Abstract

Bone (or body) morphogenetic proteins (BMPs) belong to the TGFβ superfamily and are crucial for embryonic patterning and organogenesis as well as for adult tissue homeostasis and repair. Activation of BMP receptors by their ligands leads to induction of several signaling cascades. Using fluorescence recovery after photobleaching, FRET, and single particle tracking microscopy, we demonstrate that BMP receptor type I and II (BMPRI and BMPRII) have distinct lateral mobility properties within the plasma membrane, which is mandatory for their involvement in different signaling pathways. Before ligand binding, BMPRI and a subpopulation of BMPRII exhibit confined motion, reflecting preassembled heteromeric receptor complexes. A second free diffusing BMPRII population only becomes restricted after ligand addition. This paper visualizes time-resolved BMP receptor complex formation and demonstrates that the lateral mobility of BMPRI has a major impact in stabilizing heteromeric BMPRI-BMPRII receptor complexes to differentially stimulate SMAD versus non-SMAD signaling.

Citing Articles

Endothelial tip-cell position, filopodia formation and biomechanics require BMPR2 expression and signaling.

Hiepen C, Benamar M, Barrasa-Fano J, Condor M, Ilhan M, Munch J Commun Biol. 2025; 8(1):21.

PMID: 39779836 PMC: 11711618. DOI: 10.1038/s42003-024-07431-8.


Cholesterol modulates type I/II TGF-β receptor complexes and alters the balance between Smad and Akt signaling in hepatocytes.

Chaudhary R, Goodman L, Wang S, Asimakopoulos A, Weiskirchen R, Dooley S Commun Biol. 2024; 7(1):8.

PMID: 38168942 PMC: 10761706. DOI: 10.1038/s42003-023-05654-9.


Characterization of Fibrodysplasia Ossificans Progessiva relevant Acvr1/Acvr2 Activin receptors in medaka (Oryzias latipes).

Trumpp M, Tan W, Burdzinski W, Basler Y, Jatzlau J, Knaus P PLoS One. 2023; 18(9):e0291379.

PMID: 37708126 PMC: 10501582. DOI: 10.1371/journal.pone.0291379.


A versatile Halo- and SNAP-tagged BMP/TGFβ receptor library for quantification of cell surface ligand binding.

Jatzlau J, Burdzinski W, Trumpp M, Obendorf L, Rossmann K, Ravn K Commun Biol. 2023; 6(1):34.

PMID: 36635368 PMC: 9837045. DOI: 10.1038/s42003-022-04388-4.


Integrin-based adhesion compartmentalizes ALK3 of the BMPRII to control cell adhesion and migration.

Guevara-Garcia A, Fourel L, Bourrin-Reynard I, Sales A, Oddou C, Pezet M J Cell Biol. 2022; 221(12).

PMID: 36205720 PMC: 9552562. DOI: 10.1083/jcb.202107110.


References
1.
Lee K, DAcquisto F, Hayden M, Shim J, Ghosh S . PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation. Science. 2005; 308(5718):114-8. DOI: 10.1126/science.1107107. View

2.
Kim J, Park J, Choi S, Chi S, Mowbray A, Jo H . X-linked inhibitor of apoptosis protein is an important regulator of vascular endothelial growth factor-dependent bovine aortic endothelial cell survival. Circ Res. 2008; 102(8):896-904. PMC: 8543358. DOI: 10.1161/CIRCRESAHA.107.163667. View

3.
Luga V, McLean S, Le Roy C, OConnor-Mccourt M, Wrana J, Di Guglielmo G . The extracellular domain of the TGFbeta type II receptor regulates membrane raft partitioning. Biochem J. 2009; 421(1):119-31. DOI: 10.1042/BJ20081131. View

4.
Samad T, Rebbapragada A, Bell E, Zhang Y, Sidis Y, Jeong S . DRAGON, a bone morphogenetic protein co-receptor. J Biol Chem. 2005; 280(14):14122-9. DOI: 10.1074/jbc.M410034200. View

5.
Nohe A, Keating E, Underhill T, Knaus P, Petersen N . Dynamics and interaction of caveolin-1 isoforms with BMP-receptors. J Cell Sci. 2005; 118(Pt 3):643-50. DOI: 10.1242/jcs.01402. View