Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis

Embryogenesis relies on instructions provided by spatially organized signaling molecules known as morphogens. Understanding the principles behind morphogen distribution and how cells interpret locally this information remains a major challenge in developmental biology. Here, we introduce morphogen-a...

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Autores principales:	Durrieu, L., Kirrmaier, D., Schneidt, T., Kats, I., Raghavan, S., Hufnagel, L., Saunders, T.E., Knop, M.
Formato:	JOUR
Materias:	Drosophila melanogaster embryogenesis fluorescent timers morphogen gradient SPIM morphogen protein Article diffusion coefficient Drosophila embryo embryo development model molecular dynamics nonhuman priority journal protein analysis protein degradation protein processing protein synthesis quantitative analysis signal transduction
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_17444292_v14_n9_p_Durrieu
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_17444292_v14_n9_p_Durrieu
record_format	dspace
spelling	todo:paper_17444292_v14_n9_p_Durrieu2023-10-03T16:31:47Z Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis Durrieu, L. Kirrmaier, D. Schneidt, T. Kats, I. Raghavan, S. Hufnagel, L. Saunders, T.E. Knop, M. Drosophila melanogaster embryogenesis fluorescent timers morphogen gradient SPIM morphogen protein Article diffusion coefficient Drosophila embryo embryo development model molecular dynamics nonhuman priority journal protein analysis protein degradation protein processing protein synthesis quantitative analysis signal transduction Embryogenesis relies on instructions provided by spatially organized signaling molecules known as morphogens. Understanding the principles behind morphogen distribution and how cells interpret locally this information remains a major challenge in developmental biology. Here, we introduce morphogen-age measurements as a novel approach to test models of morphogen gradient formation. Using a tandem fluorescent timer as a protein age sensor, we find a gradient of increasing age of Bicoid along the anterior–posterior axis in the early Drosophila embryo. Quantitative analysis of the protein age distribution across the embryo reveals that the synthesis–diffusion–degradation model is the most likely model underlying Bicoid gradient formation, and rules out other hypotheses for gradient formation. Moreover, we show that the timer can detect transitions in the dynamics associated with syncytial cellularization. Our results provide new insight into Bicoid gradient formation and demonstrate how morphogen-age information can complement knowledge about movement, abundance, and distribution, which should be widely applicable to other systems. © 2018 The Authors. Published under the terms of the CC BY 4.0 license JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_17444292_v14_n9_p_Durrieu
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Drosophila melanogaster embryogenesis fluorescent timers morphogen gradient SPIM morphogen protein Article diffusion coefficient Drosophila embryo embryo development model molecular dynamics nonhuman priority journal protein analysis protein degradation protein processing protein synthesis quantitative analysis signal transduction
spellingShingle	Drosophila melanogaster embryogenesis fluorescent timers morphogen gradient SPIM morphogen protein Article diffusion coefficient Drosophila embryo embryo development model molecular dynamics nonhuman priority journal protein analysis protein degradation protein processing protein synthesis quantitative analysis signal transduction Durrieu, L. Kirrmaier, D. Schneidt, T. Kats, I. Raghavan, S. Hufnagel, L. Saunders, T.E. Knop, M. Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
topic_facet	Drosophila melanogaster embryogenesis fluorescent timers morphogen gradient SPIM morphogen protein Article diffusion coefficient Drosophila embryo embryo development model molecular dynamics nonhuman priority journal protein analysis protein degradation protein processing protein synthesis quantitative analysis signal transduction
description	Embryogenesis relies on instructions provided by spatially organized signaling molecules known as morphogens. Understanding the principles behind morphogen distribution and how cells interpret locally this information remains a major challenge in developmental biology. Here, we introduce morphogen-age measurements as a novel approach to test models of morphogen gradient formation. Using a tandem fluorescent timer as a protein age sensor, we find a gradient of increasing age of Bicoid along the anterior–posterior axis in the early Drosophila embryo. Quantitative analysis of the protein age distribution across the embryo reveals that the synthesis–diffusion–degradation model is the most likely model underlying Bicoid gradient formation, and rules out other hypotheses for gradient formation. Moreover, we show that the timer can detect transitions in the dynamics associated with syncytial cellularization. Our results provide new insight into Bicoid gradient formation and demonstrate how morphogen-age information can complement knowledge about movement, abundance, and distribution, which should be widely applicable to other systems. © 2018 The Authors. Published under the terms of the CC BY 4.0 license
format	JOUR
author	Durrieu, L. Kirrmaier, D. Schneidt, T. Kats, I. Raghavan, S. Hufnagel, L. Saunders, T.E. Knop, M.
author_facet	Durrieu, L. Kirrmaier, D. Schneidt, T. Kats, I. Raghavan, S. Hufnagel, L. Saunders, T.E. Knop, M.
author_sort	Durrieu, L.
title	Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
title_short	Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
title_full	Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
title_fullStr	Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
title_full_unstemmed	Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
title_sort	bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis
url	http://hdl.handle.net/20.500.12110/paper_17444292_v14_n9_p_Durrieu
work_keys_str_mv	AT durrieul bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT kirrmaierd bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT schneidtt bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT katsi bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT raghavans bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT hufnagell bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT saunderste bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis AT knopm bicoidgradientformationmechanismanddynamicsrevealedbyproteinlifetimeanalysis
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Bicoid gradient formation mechanism and dynamics revealed by protein lifetime analysis

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