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Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors

How is information communicated both within and between cells of living systems with high signal to noise? We discuss transmembrane signaling models involving two receptor tyrosine kinases: the fibroblast growth factor receptor (FGFR) and the MET receptor. We suggest that simple dimerization models...

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Detalles Bibliográficos
Autores principales: Blaszczyk, Michal, Harmer, Nicholas J., Chirgadze, Dimitri Y., Ascher, David B., Blundell, Tom L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pergamon Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4832006/
https://www.ncbi.nlm.nih.gov/pubmed/25957048
http://dx.doi.org/10.1016/j.pbiomolbio.2015.04.007
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author Blaszczyk, Michal
Harmer, Nicholas J.
Chirgadze, Dimitri Y.
Ascher, David B.
Blundell, Tom L.
author_facet Blaszczyk, Michal
Harmer, Nicholas J.
Chirgadze, Dimitri Y.
Ascher, David B.
Blundell, Tom L.
author_sort Blaszczyk, Michal
collection PubMed
description How is information communicated both within and between cells of living systems with high signal to noise? We discuss transmembrane signaling models involving two receptor tyrosine kinases: the fibroblast growth factor receptor (FGFR) and the MET receptor. We suggest that simple dimerization models might occur opportunistically giving rise to noise but cooperative clustering of the receptor tyrosine kinases observed in these systems is likely to be important for signal transduction. We propose that this may be a more general prerequisite for high signal to noise in transmembrane receptor signaling.
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spelling pubmed-48320062016-04-25 Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors Blaszczyk, Michal Harmer, Nicholas J. Chirgadze, Dimitri Y. Ascher, David B. Blundell, Tom L. Prog Biophys Mol Biol Review How is information communicated both within and between cells of living systems with high signal to noise? We discuss transmembrane signaling models involving two receptor tyrosine kinases: the fibroblast growth factor receptor (FGFR) and the MET receptor. We suggest that simple dimerization models might occur opportunistically giving rise to noise but cooperative clustering of the receptor tyrosine kinases observed in these systems is likely to be important for signal transduction. We propose that this may be a more general prerequisite for high signal to noise in transmembrane receptor signaling. Pergamon Press 2015-09 /pmc/articles/PMC4832006/ /pubmed/25957048 http://dx.doi.org/10.1016/j.pbiomolbio.2015.04.007 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Blaszczyk, Michal
Harmer, Nicholas J.
Chirgadze, Dimitri Y.
Ascher, David B.
Blundell, Tom L.
Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors
title Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors
title_full Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors
title_fullStr Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors
title_full_unstemmed Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors
title_short Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors
title_sort achieving high signal-to-noise in cell regulatory systems: spatial organization of multiprotein transmembrane assemblies of fgfr and met receptors
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4832006/
https://www.ncbi.nlm.nih.gov/pubmed/25957048
http://dx.doi.org/10.1016/j.pbiomolbio.2015.04.007
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