Intricacies of BMP receptor assembly. Academic Article

abstract

• The TGF-beta superfamily exhibits a feature making it distinct from many other growth factor families in that the inadequate number of ligands and receptors premises a high degree of promiscuity in ligand-receptor interaction. This highlights the importance of even small differences in affinities and specificities between different binding partners to maintain the broad spectrum of their well defined biological functions. Despite the promiscuous interactions recent data reveal differences in receptor recruitment, architectures of these assemblies and specific modulation by a multitude of extracellular as well as membrane-associated factors. These modulatory mechanisms might possibly add specificity towards defined biological functions despite the overlapping usage of receptors by various ligands.

authors

• Groppe, Jay

published proceedings

• Cytokine Growth Factor Rev

altmetric score

• 3

author list (cited authors)

• Nickel, J., Sebald, W., Groppe, J. C., & Mueller, T. D.

citation count

• 83

complete list of authors

• Nickel, Joachim||Sebald, Walter||Groppe, Jay C||Mueller, Thomas D

publication date

• October 2009

publisher

• Elsevier  Publisher

published in

• Cytokine and Growth Factor Reviews  Journal

keywords

• Animals
• Bone Morphogenetic Protein Receptors
• Humans
• Models, Biological
• Models, Molecular
• Protein Multimerization
• Structure-Activity Relationship
• Tgf-beta Superfamily Proteins

PubMed Central ID

• 19926516

Digital Object Identifier (DOI)

• 10.1016/j.cytogfr.2009.10.022

start page

• 367

end page

• 377

volume

• 20

issue

• 5-6

URL

• http://dx.doi.org/10.1016/j.cytogfr.2009.10.022