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How to assemble a scale-invariant gradient

Intracellular protein gradients serve a variety of functions, such as the establishment of cell polarity or to provide positional information for gene expression in developing embryos. Given that cell size in a population can vary considerably, for the protein gradients to work properly they often h...

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Detalles Bibliográficos
Autores principales: Datta, Arnab, Ghosh, Sagnik, Kondev, Jane
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8986316/
https://www.ncbi.nlm.nih.gov/pubmed/35311649
http://dx.doi.org/10.7554/eLife.71365
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author Datta, Arnab
Ghosh, Sagnik
Kondev, Jane
author_facet Datta, Arnab
Ghosh, Sagnik
Kondev, Jane
author_sort Datta, Arnab
collection PubMed
description Intracellular protein gradients serve a variety of functions, such as the establishment of cell polarity or to provide positional information for gene expression in developing embryos. Given that cell size in a population can vary considerably, for the protein gradients to work properly they often have to be scaled to the size of the cell. Here, we examine a model of protein gradient formation within a cell that relies on cytoplasmic diffusion and cortical transport of proteins toward a cell pole. We show that the shape of the protein gradient is determined solely by the cell geometry. Furthermore, we show that the length scale over which the protein concentration in the gradient varies is determined by the linear dimensions of the cell, independent of the diffusion constant or the transport speed. This gradient provides scale-invariant positional information within a cell, which can be used for assembly of intracellular structures whose size is scaled to the linear dimensions of the cell, such as the cytokinetic ring and actin cables in budding yeast cells.
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spelling pubmed-89863162022-04-07 How to assemble a scale-invariant gradient Datta, Arnab Ghosh, Sagnik Kondev, Jane eLife Physics of Living Systems Intracellular protein gradients serve a variety of functions, such as the establishment of cell polarity or to provide positional information for gene expression in developing embryos. Given that cell size in a population can vary considerably, for the protein gradients to work properly they often have to be scaled to the size of the cell. Here, we examine a model of protein gradient formation within a cell that relies on cytoplasmic diffusion and cortical transport of proteins toward a cell pole. We show that the shape of the protein gradient is determined solely by the cell geometry. Furthermore, we show that the length scale over which the protein concentration in the gradient varies is determined by the linear dimensions of the cell, independent of the diffusion constant or the transport speed. This gradient provides scale-invariant positional information within a cell, which can be used for assembly of intracellular structures whose size is scaled to the linear dimensions of the cell, such as the cytokinetic ring and actin cables in budding yeast cells. eLife Sciences Publications, Ltd 2022-03-21 /pmc/articles/PMC8986316/ /pubmed/35311649 http://dx.doi.org/10.7554/eLife.71365 Text en © 2022, Datta et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Physics of Living Systems
Datta, Arnab
Ghosh, Sagnik
Kondev, Jane
How to assemble a scale-invariant gradient
title How to assemble a scale-invariant gradient
title_full How to assemble a scale-invariant gradient
title_fullStr How to assemble a scale-invariant gradient
title_full_unstemmed How to assemble a scale-invariant gradient
title_short How to assemble a scale-invariant gradient
title_sort how to assemble a scale-invariant gradient
topic Physics of Living Systems
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8986316/
https://www.ncbi.nlm.nih.gov/pubmed/35311649
http://dx.doi.org/10.7554/eLife.71365
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