Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.

<h4>Background</h4>Normal cell function requires timely and accurate transmission of information from receptors on the cell membrane (CM) to the nucleus. Movement of messenger proteins in the cytoplasm is thought to be dependent on random walk. However, Brownian motion will disperse mess...

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Autores principales:	Robert A Gatenby, B Roy Frieden
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a4bfae97e51a467d88829a6e403f17b3
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spelling	oai:doaj.org-article:a4bfae97e51a467d88829a6e403f17b32021-11-18T06:36:11ZCoulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.1932-620310.1371/journal.pone.0012084https://doaj.org/article/a4bfae97e51a467d88829a6e403f17b32010-08-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20711447/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Normal cell function requires timely and accurate transmission of information from receptors on the cell membrane (CM) to the nucleus. Movement of messenger proteins in the cytoplasm is thought to be dependent on random walk. However, Brownian motion will disperse messenger proteins throughout the cytosol resulting in slow and highly variable transit times. We propose that a critical component of information transfer is an intracellular electric field generated by distribution of charge on the nuclear membrane (NM). While the latter has been demonstrated experimentally for decades, the role of the consequent electric field has been assumed to be minimal due to a Debye length of about 1 nanometer that results from screening by intracellular Cl- and K+. We propose inclusion of these inorganic ions in the Debye-Huckel equation is incorrect because nuclear pores allow transit through the membrane at a rate far faster than the time to thermodynamic equilibrium. In our model, only the charged, mobile messenger proteins contribute to the Debye length.<h4>Findings</h4>Using this revised model and published data, we estimate the NM possesses a Debye-Huckel length of a few microns and find this is consistent with recent measurement using intracellular nano-voltmeters. We demonstrate the field will accelerate isolated messenger proteins toward the nucleus through Coulomb interactions with negative charges added by phosphorylation. We calculate transit times as short as 0.01 sec. When large numbers of phosphorylated messenger proteins are generated by increasing concentrations of extracellular ligands, we demonstrate they generate a self-screening environment that regionally attenuates the cytoplasmic field, slowing movement but permitting greater cross talk among pathways. Preliminary experimental results with phosphorylated RAF are consistent with model predictions.<h4>Conclusion</h4>This work demonstrates that previously unrecognized Coulomb interactions between phosphorylated messenger proteins and intracellular electric fields will optimize information transfer from the CM to the NM in cells.Robert A GatenbyB Roy FriedenPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 8, p e12084 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Robert A Gatenby B Roy Frieden Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
description	<h4>Background</h4>Normal cell function requires timely and accurate transmission of information from receptors on the cell membrane (CM) to the nucleus. Movement of messenger proteins in the cytoplasm is thought to be dependent on random walk. However, Brownian motion will disperse messenger proteins throughout the cytosol resulting in slow and highly variable transit times. We propose that a critical component of information transfer is an intracellular electric field generated by distribution of charge on the nuclear membrane (NM). While the latter has been demonstrated experimentally for decades, the role of the consequent electric field has been assumed to be minimal due to a Debye length of about 1 nanometer that results from screening by intracellular Cl- and K+. We propose inclusion of these inorganic ions in the Debye-Huckel equation is incorrect because nuclear pores allow transit through the membrane at a rate far faster than the time to thermodynamic equilibrium. In our model, only the charged, mobile messenger proteins contribute to the Debye length.<h4>Findings</h4>Using this revised model and published data, we estimate the NM possesses a Debye-Huckel length of a few microns and find this is consistent with recent measurement using intracellular nano-voltmeters. We demonstrate the field will accelerate isolated messenger proteins toward the nucleus through Coulomb interactions with negative charges added by phosphorylation. We calculate transit times as short as 0.01 sec. When large numbers of phosphorylated messenger proteins are generated by increasing concentrations of extracellular ligands, we demonstrate they generate a self-screening environment that regionally attenuates the cytoplasmic field, slowing movement but permitting greater cross talk among pathways. Preliminary experimental results with phosphorylated RAF are consistent with model predictions.<h4>Conclusion</h4>This work demonstrates that previously unrecognized Coulomb interactions between phosphorylated messenger proteins and intracellular electric fields will optimize information transfer from the CM to the NM in cells.
format	article
author	Robert A Gatenby B Roy Frieden
author_facet	Robert A Gatenby B Roy Frieden
author_sort	Robert A Gatenby
title	Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
title_short	Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
title_full	Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
title_fullStr	Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
title_full_unstemmed	Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
title_sort	coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/a4bfae97e51a467d88829a6e403f17b3
work_keys_str_mv	AT robertagatenby coulombinteractionsbetweencytoplasmicelectricfieldsandphosphorylatedmessengerproteinsoptimizeinformationflowincells AT broyfrieden coulombinteractionsbetweencytoplasmicelectricfieldsandphosphorylatedmessengerproteinsoptimizeinformationflowincells
_version_	1718424433912184832

Coulomb interactions between cytoplasmic electric fields and phosphorylated messenger proteins optimize information flow in cells.

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