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Article ; Online: Mactosylceramide prevents glial cell overgrowth by inhibiting insulin and fibroblast growth factor receptor signaling.

Gerdøe-Kristensen, Stine / Lund, Viktor K / Wandall, Hans H / Kjaerulff, Ole

2017 Volume 232, Issue 11, Page(s) 3112–3127

Abstract: Receptor tyrosine kinase (RTK) signaling controls key aspects of cellular differentiation, proliferation, survival, metabolism, and migration. Deregulated RTK signaling also underlies many cancers. Glycosphingolipids (GSL) are essential elements of the ... ...

Abstract	Receptor tyrosine kinase (RTK) signaling controls key aspects of cellular differentiation, proliferation, survival, metabolism, and migration. Deregulated RTK signaling also underlies many cancers. Glycosphingolipids (GSL) are essential elements of the plasma membrane. By affecting clustering and activity of membrane receptors, GSL modulate signal transduction, including that mediated by the RTK. GSL are abundant in the nervous system, and glial development in Drosophila is emerging as a useful model for studying how GSL modulate RTK signaling. Drosophila has a simple GSL biosynthetic pathway, in which the mannosyltransferase Egghead controls conversion of glucosylceramide (GlcCer) to mactosylceramide (MacCer). Lack of elongated GSL in egghead (egh) mutants causes overgrowth of subperineurial glia (SPG), largely due to aberrant activation of phosphatidylinositol 3-kinase (PI3K). However, to what extent this effect involves changes in upstream signaling events is unresolved. We show here that glial overgrowth in egh is strongly linked to increased activation of Insulin and fibroblast growth factor receptors (FGFR). Glial hypertrophy is phenocopied when overexpressing gain-of-function mutants of the Drosophila insulin receptor (InR) and the FGFR homolog Heartless (Htl) in wild type SPG, and is suppressed by inhibiting Htl and InR activity in egh. Knockdown of GlcCer synthase in the SPG fails to suppress glial overgrowth in egh nerves, and slightly promotes overgrowth in wild type, suggesting that RTK hyperactivation is caused by absence of MacCer and not by GlcCer accumulation. We conclude that an early product in GSL biosynthesis, MacCer, prevents inappropriate activation of insulin and fibroblast growth factor receptors in Drosophila glia.
MeSH term(s)	Animals ; Animals, Genetically Modified ; Cell Enlargement ; Ceramides/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/genetics ; Drosophila melanogaster/immunology ; Drosophila melanogaster/metabolism ; Galactosyltransferases/genetics ; Galactosyltransferases/metabolism ; Genotype ; Hypertrophy ; Ligands ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mutation ; Neuroglia/immunology ; Neuroglia/metabolism ; Neuroglia/pathology ; Phenotype ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/metabolism ; Receptor Protein-Tyrosine Kinases/genetics ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, Fibroblast Growth Factor/genetics ; Receptors, Fibroblast Growth Factor/metabolism ; Signal Transduction
Chemical Substances	Ceramides ; Drosophila Proteins ; Ligands ; Membrane Proteins ; Receptors, Fibroblast Growth Factor ; brn protein, Drosophila ; egh protein, Drosophila ; flotillins ; Galactosyltransferases (EC 2.4.1.-) ; glucosylceramide beta-1-4-galactosyltransferase (EC 2.4.1.-) ; InR protein, Drosophila (EC 2.7.10.1) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; htl protein, Drosophila (EC 2.7.10.1)
Language	English
Publishing date	2017-03-31
Publishing country	United States
Document type	Journal Article
ZDB-ID	3116-1
ISSN	1097-4652 ; 0021-9541
ISSN (online)	1097-4652
ISSN	0021-9541
DOI	10.1002/jcp.25762
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Article ; Online: Regulation of Toll and Toll-like receptor signaling by the endocytic pathway.

Lund, Viktor K / Delotto, Robert

Small GTPases

2011 Volume 2, Issue 2, Page(s) 95–98

Abstract: The Toll/TLR receptor family plays a central role in both vertebrate and insect immunity, driving the activation of humoral immunity in response to pathogens. In Drosophila, Toll is also responsible for directing the formation of the Dorsal/NFkappaB ... ...

Abstract	The Toll/TLR receptor family plays a central role in both vertebrate and insect immunity, driving the activation of humoral immunity in response to pathogens. In Drosophila, Toll is also responsible for directing the formation of the Dorsal/NFkappaB gradient specifying dorsoventral patterning of the embryo. Two recent studies have revealed that endocytosis and elements of the molecular machinery governing endosomal progression are required for Drosophila Toll signaling in development and immunity. We demonstrated that Toll is not only present at the plasma membrane but also in a Rab5(+) early endosomal compartment in the embryo and that the distribution of constitutively active Toll(10B) is shifted towards endosomes. Localized inhibition of Rab5 function on the ventral side leads to a reduction of nuclear Dorsal levels, while locally increasing Rab5 function leads to potentiation of signaling. Independently, another laboratory identified the endosomal protein Mop as a potentiator of Toll signaling in Drosophila cell culture and fat-body tissue. Mop functions together with the ESCRT 0 component, Hrs, previously reported to stimulate endosomal progression and the signaling ability of internalized EGFR. We discuss these studies and briefly summarize the most significant findings concerning the role of intracellular localization and trafficking in mammalian TLR function.
Language	English
Publishing date	2011-06-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	2682247-7
ISSN	2154-1256 ; 2154-1248
ISSN (online)	2154-1256
ISSN	2154-1248
DOI	10.4161/sgtp.2.2.15378
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Article ; Online: Coding variants identified in patients with diabetes alter PICK1 BAR domain function in insulin granule biogenesis.

The Journal of clinical investigation

2022 Volume 132, Issue 5

Abstract: Bin/amphiphysin/Rvs (BAR) domains are positively charged crescent-shaped modules that mediate curvature of negatively charged lipid membranes during remodeling processes. The BAR domain proteins PICK1, ICA69, and the arfaptins have recently been ... ...

Abstract	Bin/amphiphysin/Rvs (BAR) domains are positively charged crescent-shaped modules that mediate curvature of negatively charged lipid membranes during remodeling processes. The BAR domain proteins PICK1, ICA69, and the arfaptins have recently been demonstrated to coordinate the budding and formation of immature secretory granules (ISGs) at the trans-Golgi network. Here, we identify 4 coding variants in the PICK1 gene from a whole-exome screening of Danish patients with diabetes that each involve a change in positively charged residues in the PICK1 BAR domain. All 4 coding variants failed to rescue insulin content in INS-1E cells upon knock down of endogenous PICK1. Moreover, 2 variants showed dominant-negative properties. In vitro assays addressing BAR domain function suggested that the coding variants compromised BAR domain function but increased the capacity to cause fission of liposomes. Live confocal microscopy and super-resolution microscopy further revealed that PICK1 resides transiently on ISGs before egress via vesicular budding events. Interestingly, this egress of PICK1 was accelerated in the coding variants. We propose that PICK1 assists in or complements the removal of excess membrane and generic membrane trafficking proteins, and possibly also insulin, from ISGs during the maturation process; and that the coding variants may cause premature budding, possibly explaining their dominant-negative function.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Carrier Proteins/genetics ; Cell Membrane/metabolism ; Diabetes Mellitus/genetics ; Diabetes Mellitus/metabolism ; Humans ; Insulin/genetics ; Insulin/metabolism ; Nerve Tissue Proteins ; Nuclear Proteins/metabolism ; Protein Binding
Chemical Substances	Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Insulin ; Nerve Tissue Proteins ; Nuclear Proteins ; PICk1 protein, human ; amphiphysin (147954-52-7)
Language	English
Publishing date	2022-03-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3067-3
ISSN	1558-8238 ; 0021-9738
ISSN (online)	1558-8238
ISSN	0021-9738
DOI	10.1172/JCI144904
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Article ; Online: Identifying dominant-negative actions of a dopamine transporter variant in patients with parkinsonism and neuropsychiatric disease.

Herborg, Freja / Jensen, Kathrine L / Tolstoy, Sasha / Arends, Natascha V / Posselt, Leonie P / Shekar, Aparna / Aguilar, Jenny I / Lund, Viktor K / Erreger, Kevin / Rickhag, Mattias / Lycas, Matthew D / Lonsdale, Markus N / Rahbek-Clemmensen, Troels / Sørensen, Andreas T / Newman, Amy H / Løkkegaard, Annemette / Kjærulff, Ole / Werge, Thomas / Møller, Lisbeth B /

Matthies, Heinrich Jg / Galli, Aurelio / Hjermind, Lena E / Gether, Ulrik

JCI insight

2021 Volume 6, Issue 18

Abstract: Dysfunctional dopaminergic neurotransmission is central to movement disorders and mental diseases. The dopamine transporter (DAT) regulates extracellular dopamine levels, but the genetic and mechanistic link between DAT function and dopamine-related ... ...

Abstract	Dysfunctional dopaminergic neurotransmission is central to movement disorders and mental diseases. The dopamine transporter (DAT) regulates extracellular dopamine levels, but the genetic and mechanistic link between DAT function and dopamine-related pathologies is not clear. Particularly, the pathophysiological significance of monoallelic missense mutations in DAT is unknown. Here, we use clinical information, neuroimaging, and large-scale exome-sequencing data to uncover the occurrence and phenotypic spectrum of a DAT coding variant, DAT-K619N, which localizes to the critical C-terminal PSD-95/Discs-large/ZO-1 homology-binding motif of human DAT (hDAT). We identified the rare but recurrent hDAT-K619N variant in exome-sequenced samples of patients with neuropsychiatric diseases and a patient with early-onset neurodegenerative parkinsonism and comorbid neuropsychiatric disease. In cell cultures, hDAT-K619N displayed reduced uptake capacity, decreased surface expression, and accelerated turnover. Unilateral expression in mouse nigrostriatal neurons revealed differential effects of hDAT-K619N and hDAT-WT on dopamine-directed behaviors, and hDAT-K619N expression in Drosophila led to impairments in dopamine transmission with accompanying hyperlocomotion and age-dependent disturbances of the negative geotactic response. Moreover, cellular studies and viral expression of hDAT-K619N in mice demonstrated a dominant-negative effect of the hDAT-K619N mutant. Summarized, our results suggest that hDAT-K619N can effectuate dopamine dysfunction of pathological relevance in a dominant-negative manner.
MeSH term(s)	Adult ; Animals ; Behavior, Animal ; Biological Transport ; Cells, Cultured ; Databases, Genetic ; Dopamine/metabolism ; Dopamine Plasma Membrane Transport Proteins/genetics ; Dopamine Plasma Membrane Transport Proteins/metabolism ; Drosophila ; Exome ; Female ; Humans ; Hypokinesia/diagnostic imaging ; Hypokinesia/genetics ; Hypokinesia/metabolism ; Male ; Mental Disorders/genetics ; Mental Disorders/metabolism ; Mesencephalon/metabolism ; Mice ; Middle Aged ; Motor Activity/genetics ; Mutation ; Neurons/metabolism ; Parkinsonian Disorders/diagnostic imaging ; Parkinsonian Disorders/genetics ; Parkinsonian Disorders/metabolism ; Phenotype ; Synaptic Transmission ; Tomography, Emission-Computed, Single-Photon ; Transfection
Chemical Substances	Dopamine Plasma Membrane Transport Proteins ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2021-09-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.151496
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Article ; Online: Endocytosis is required for Toll signaling and shaping of the Dorsal/NF-kappaB morphogen gradient during Drosophila embryogenesis.

Lund, Viktor K / DeLotto, Yvonne / DeLotto, Robert

Proceedings of the National Academy of Sciences of the United States of America

2010 Volume 107, Issue 42, Page(s) 18028–18033

Abstract: Dorsoventral cell fate in the Drosophila embryo is specified by activation of the Toll receptor, leading to a ventral-to-dorsal gradient across nuclei of the NF-κB transcription factor Dorsal. Toll receptor has been investigated genetically, molecularly, ...

Abstract	Dorsoventral cell fate in the Drosophila embryo is specified by activation of the Toll receptor, leading to a ventral-to-dorsal gradient across nuclei of the NF-κB transcription factor Dorsal. Toll receptor has been investigated genetically, molecularly, and immunohistologically, but much less is known about its dynamics in living embryos. Using live imaging of fluorescent protein chimeras, we find that Toll is recruited from the plasma membrane to Rab5(+) early endosomes. The distribution of a constitutively active form of Toll, Toll(10b), is shifted from the plasma membrane to early endosomes. Inhibition of endocytosis on the ventral side of the embryo attenuates Toll signaling ventrally and causes Dorsal to accumulate on the dorsal side of the embryo, essentially inverting the dorsal/ventral axis. Conversely, enhancing endocytosis laterally greatly potentiates Toll signaling locally, altering the shape of the Dorsal gradient. Photoactivation and fluorescence recovery after photobleaching studies reveal that Toll exhibits extremely limited lateral diffusion within the plasma membrane, whereas Toll is highly compartmentalized in endosomes. When endocytosis is blocked ventrally, creating an ectopic dorsal signaling center, Toll is preferentially endocytosed at the ectopic signaling center. We propose that Toll signals from an endocytic compartment rather than the plasma membrane. Our studies reveal that endocytosis plays a pivotal role in the spatial regulation of Toll receptor activation and signaling and in the correct shaping of the nuclear Dorsal concentration gradient.
MeSH term(s)	Animals ; Base Sequence ; Body Patterning ; Cell Membrane/metabolism ; DNA, Complementary ; Drosophila/embryology ; Drosophila Proteins/metabolism ; Endocytosis ; Endosomes/metabolism ; Green Fluorescent Proteins/metabolism ; NF-kappa B/metabolism ; Nuclear Proteins/metabolism ; Phosphoproteins/metabolism ; Signal Transduction ; Toll-Like Receptors/metabolism ; Transcription Factors/metabolism
Chemical Substances	DNA, Complementary ; Drosophila Proteins ; NF-kappa B ; Nuclear Proteins ; Phosphoproteins ; Toll-Like Receptors ; Transcription Factors ; dl protein, Drosophila ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2010-10-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1009157107
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Article: A set of P-element transformation vectors permitting the simplified generation of fluorescent fusion proteins in Drosophila melanogaster

Lund, Viktor K / DeLotto, Yvonne / DeLotto, Robert

Fly. 2011 July 1, v. 5, no. 3

2011

Abstract: We have assembled a molecular toolkit enabling the facile generation of C-terminal fluorescent protein fusion constructs for the construction of transgenic Drosophila lines in the form of a series of modified vectors for P-element transformation. These ... ...

Abstract	We have assembled a molecular toolkit enabling the facile generation of C-terminal fluorescent protein fusion constructs for the construction of transgenic Drosophila lines in the form of a series of modified vectors for P-element transformation. These vectors contain one of a variety of fluorescent tags including GFP, mCherry, Venus, Cerulean, photoactivatable paGFP and the red-to-green photoconvertible protein Dendra and provide a range of options with respect to transcriptional regulation. The vectors have been extensively tested in vivo and can produce fluorescent chimeric proteins that are functional.
Keywords	Drosophila melanogaster ; fluorescence ; genetically modified organisms ; recombinant fusion proteins ; transcription (genetics)
Language	English
Dates of publication	2011-0701
Size	p. 255-260.
Publishing place	Taylor & Francis
Document type	Article
Note	NAL-light
ISSN	1933-6942
DOI	10.4161/fly.5.3.15244
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Article: Endocytosis is required for Toll signaling and shaping of the Dorsal/NF-κB morphogen gradient during Drosophila embryogenesis

Lund, Viktor K / DeLotto, Yvonne / DeLotto, Robert

Proceedings of the National Academy of Sciences of the United States of America. 2010 Oct. 19, v. 107, no. 42

2010

Abstract	Dorsoventral cell fate in the Drosophila embryo is specified by activation of the Toll receptor, leading to a ventral-to-dorsal gradient across nuclei of the NF-κB transcription factor Dorsal. Toll receptor has been investigated genetically, molecularly, and immunohistologically, but much less is known about its dynamics in living embryos. Using live imaging of fluorescent protein chimeras, we find that Toll is recruited from the plasma membrane to Rab5⁺ early endosomes. The distribution of a constitutively active form of Toll, Toll¹⁰b, is shifted from the plasma membrane to early endosomes. Inhibition of endocytosis on the ventral side of the embryo attenuates Toll signaling ventrally and causes Dorsal to accumulate on the dorsal side of the embryo, essentially inverting the dorsal/ventral axis. Conversely, enhancing endocytosis laterally greatly potentiates Toll signaling locally, altering the shape of the Dorsal gradient. Photoactivation and fluorescence recovery after photobleaching studies reveal that Toll exhibits extremely limited lateral diffusion within the plasma membrane, whereas Toll is highly compartmentalized in endosomes. When endocytosis is blocked ventrally, creating an ectopic dorsal signaling center, Toll is preferentially endocytosed at the ectopic signaling center. We propose that Toll signals from an endocytic compartment rather than the plasma membrane. Our studies reveal that endocytosis plays a pivotal role in the spatial regulation of Toll receptor activation and signaling and in the correct shaping of the nuclear Dorsal concentration gradient.
Keywords	Drosophila ; chimerism ; embryogenesis ; endocytosis ; endosomes ; fluorescence recovery after photobleaching ; fluorescent proteins ; image analysis ; plasma membrane ; transcription factor NF-kappa B
Language	English
Dates of publication	2010-1019
Size	p. 18028-18033.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1009157107
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Article ; Online: An Amphipathic Helix Directs Cellular Membrane Curvature Sensing and Function of the BAR Domain Protein PICK1.

Cell reports

2018 Volume 23, Issue 7, Page(s) 2056–2069

Abstract: BAR domains are dimeric protein modules that sense, induce, and stabilize lipid membrane curvature. Here, we show that membrane curvature sensing (MCS) directs cellular localization and function of the BAR domain protein PICK1. In PICK1, and the ... ...

Abstract	BAR domains are dimeric protein modules that sense, induce, and stabilize lipid membrane curvature. Here, we show that membrane curvature sensing (MCS) directs cellular localization and function of the BAR domain protein PICK1. In PICK1, and the homologous proteins ICA69 and arfaptin2, we identify an amphipathic helix N-terminal to the BAR domain that mediates MCS. Mutational disruption of the helix in PICK1 impaired MCS without affecting membrane binding per se. In insulin-producing INS-1E cells, super-resolution microscopy revealed that disruption of the helix selectively compromised PICK1 density on insulin granules of high curvature during their maturation. This was accompanied by reduced hormone storage in the INS-1E cells. In Drosophila, disruption of the helix compromised growth regulation. By demonstrating size-dependent binding on insulin granules, our finding highlights the function of MCS for BAR domain proteins in a biological context distinct from their function, e.g., at the plasma membrane during endocytosis.
MeSH term(s)	Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasmic Granules/metabolism ; Drosophila Proteins/chemistry ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Insulin/metabolism ; Insulin Secretion ; Liposomes ; Protein Binding ; Protein Domains ; Protein Structure, Secondary ; Structure-Activity Relationship
Chemical Substances	Carrier Proteins ; Drosophila Proteins ; Insulin ; Liposomes ; PICK1 protein, Drosophila
Language	English
Publishing date	2018-05-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2018.04.074
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Article ; Online: Dynamics of the Dorsal morphogen gradient.

Kanodia, Jitendra S / Rikhy, Richa / Kim, Yoosik / Lund, Viktor K / DeLotto, Robert / Lippincott-Schwartz, Jennifer / Shvartsman, Stanislav Y

Proceedings of the National Academy of Sciences of the United States of America

2009 Volume 106, Issue 51, Page(s) 21707–21712

Abstract: The dorsoventral (DV) patterning of the Drosophila embryo depends on the nuclear localization gradient of Dorsal (Dl), a protein related to the mammalian NF-kappaB transcription factors. Current understanding of how the Dl gradient works has been derived ...

Abstract	The dorsoventral (DV) patterning of the Drosophila embryo depends on the nuclear localization gradient of Dorsal (Dl), a protein related to the mammalian NF-kappaB transcription factors. Current understanding of how the Dl gradient works has been derived from studies of its transcriptional interpretation, but the gradient itself has not been quantified. In particular, it is not known whether the Dl gradient is stable or dynamic during the DV patterning of the embryo. To address this question, we developed a mathematical model of the Dl gradient and constrained its parameters by experimental data. Based on our computational analysis, we predict that the Dl gradient is dynamic and, to a first approximation, can be described as a concentration profile with increasing amplitude and constant shape. These time-dependent properties of the Dl gradient are different from those of the Bicoid and MAPK phosphorylation gradients, which pattern the anterior and terminal regions of the embryo. Specifically, the gradient of the nuclear levels of Bicoid is stable, whereas the pattern of MAPK phosphorylation changes in both shape and amplitude. We attribute these striking differences in the dynamics of maternal morphogen gradients to the differences in the initial conditions and chemistries of the anterior, DV, and terminal systems.
MeSH term(s)	Animals ; Body Patterning ; Cell Nucleus/metabolism ; Drosophila/embryology ; Drosophila Proteins/metabolism ; Homeodomain Proteins/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Nuclear Proteins/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Trans-Activators/metabolism ; Transcription Factors/metabolism
Chemical Substances	Drosophila Proteins ; Homeodomain Proteins ; Nuclear Proteins ; Phosphoproteins ; Trans-Activators ; Transcription Factors ; bcd protein, Drosophila ; dl protein, Drosophila ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2009-12-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0912395106
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Article: Dynamics of the Dorsal morphogen gradient

Kanodia, Jitendra S / Rikhy, Richa / Kim, Yoosik / Lund, Viktor K / DeLotto, Robert / Lippincott-Schwartz, Jennifer / Shvartsman, Stanislav Y

Proceedings of the National Academy of Sciences of the United States of America. 2009 Dec. 22, v. 106, no. 51

2009

Abstract: The dorsoventral (DV) patterning of the Drosophila embryo depends on the nuclear localization gradient of Dorsal (Dl), a protein related to the mammalian NF-κB transcription factors. Current understanding of how the Dl gradient works has been derived ... ...

Abstract	The dorsoventral (DV) patterning of the Drosophila embryo depends on the nuclear localization gradient of Dorsal (Dl), a protein related to the mammalian NF-κB transcription factors. Current understanding of how the Dl gradient works has been derived from studies of its transcriptional interpretation, but the gradient itself has not been quantified. In particular, it is not known whether the Dl gradient is stable or dynamic during the DV patterning of the embryo. To address this question, we developed a mathematical model of the Dl gradient and constrained its parameters by experimental data. Based on our computational analysis, we predict that the Dl gradient is dynamic and, to a first approximation, can be described as a concentration profile with increasing amplitude and constant shape. These time-dependent properties of the Dl gradient are different from those of the Bicoid and MAPK phosphorylation gradients, which pattern the anterior and terminal regions of the embryo. Specifically, the gradient of the nuclear levels of Bicoid is stable, whereas the pattern of MAPK phosphorylation changes in both shape and amplitude. We attribute these striking differences in the dynamics of maternal morphogen gradients to the differences in the initial conditions and chemistries of the anterior, DV, and terminal systems.
Keywords	Drosophila melanogaster ; embryogenesis ; transcription factors ; gene expression regulation ; spatial variation ; cell nucleus ; cytochemistry ; mitogen-activated protein kinase ; protein phosphorylation
Language	English
Dates of publication	2009-1222
Size	p. 21707-21712.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
Database	NAL-Catalogue (AGRICOLA)

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