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Article ; Online: Suzanne Eaton: the beautiful logic of development.

Eaton, Suzanne

2013 Volume 202, Issue 2, Page(s) 184–185

MeSH term(s)	Animals ; Cell Biology ; Cell Polarity ; Drosophila/cytology ; Drosophila/growth & development ; Drosophila/metabolism ; Drosophila Proteins/metabolism ; Endocytosis ; Hedgehog Proteins/metabolism ; Imaginal Discs/cytology ; Imaginal Discs/metabolism ; Lipoproteins/metabolism ; Morphogenesis ; Transcription, Genetic
Chemical Substances	Drosophila Proteins ; Hedgehog Proteins ; Lipoproteins ; hh protein, Drosophila (149291-21-4)
Language	English
Publishing date	2013-07-22
Publishing country	United States
Document type	Interview ; Portrait
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.2022pi
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Article ; Online: A local insulin reservoir in Drosophila alpha cell homologs ensures developmental progression under nutrient shortage.

Ghosh, Suhrid / Leng, Weihua / Wilsch-Bräuninger, Michaela / Barrera-Velázquez, Mariana / Léopold, Pierre / Eaton, Suzanne

Current biology : CB

2022 Volume 32, Issue 8, Page(s) 1788–1797.e5

Abstract: Insulin/insulin-like growth factor (IGF) signaling (IIS) controls many aspects of development and physiology. In Drosophila, a conserved family of insulin-like peptides called Dilps is produced by brain neurosecretory cells, and it regulates organismal ... ...

Abstract	Insulin/insulin-like growth factor (IGF) signaling (IIS) controls many aspects of development and physiology. In Drosophila, a conserved family of insulin-like peptides called Dilps is produced by brain neurosecretory cells, and it regulates organismal growth and developmental timing. To accomplish these systemic functions, the Dilps are secreted into the general circulation, and they signal to peripheral tissues in an endocrine fashion. Here, we describe the local uptake and storage of Dilps in the corpora cardiaca (CC), an endocrine organ composed of alpha cell homologs known to produce the glucagon-like adipokinetic hormone (AKH). We show that Dilp uptake by the CC relies on the expression of an IGF-binding protein called ImpL2. Following their uptake, immunogold staining demonstrates that Dilps are co-packaged with AKH in dense-core vesicles for secretion. In response to nutrient shortage, this specific Dilp reservoir is released and activates IIS in a paracrine manner in the prothoracic gland. This stimulates the production of the steroid hormone ecdysone and initiates entry into pupal development. We therefore uncover a sparing mechanism whereby insulin stores in CC serve to locally activate IIS and the production of ecdysone in the PG, accelerating developmental progression in adverse food conditions.
MeSH term(s)	Animals ; Drosophila/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Ecdysone/metabolism ; Insulin/metabolism ; Insulin-Like Growth Factor Binding Proteins/metabolism ; Larva/metabolism ; Nutrients ; Somatomedins/metabolism
Chemical Substances	Drosophila Proteins ; ImpL2 protein, Drosophila ; Insulin ; Insulin-Like Growth Factor Binding Proteins ; Somatomedins ; Ecdysone (3604-87-3)
Language	English
Publishing date	2022-03-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2022.02.068
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Article ; Online: Emergence of tissue shape changes from collective cell behaviours.

Jülicher, Frank / Eaton, Suzanne

Seminars in cell & developmental biology

2017 Volume 67, Page(s) 103–112

Abstract: Anyone watching a movie of embryonic development immediately appreciates the importance of morphogenetic movements and cell flows that reshape tissue. Dynamic tissue shape changes are genetically choreographed, but their execution is essentially a ... ...

Abstract	Anyone watching a movie of embryonic development immediately appreciates the importance of morphogenetic movements and cell flows that reshape tissue. Dynamic tissue shape changes are genetically choreographed, but their execution is essentially a mechanical event. How the interplay between genetics and tissue mechanics controls tissue shape is a fundamental question. Key insights into this problem have emerged from studies in different model organisms as well as in cultured epithelia. These studies have revealed how gene expression patterns can generate patterns of planar cell polarity that orient cellular force generation and give rise to anisotropic mechanical properties of cells and tissues. These can autonomously bias the rate and orientation of cellular events such as cell divisions, extrusions, neighbor exchanges and shape changes that drive morphogenesis. However recent studies also highlight how autonomously controlled cell dynamics lead to tissue-wide stress patterns framed by mechanical constraints such as cellular connections to extracellular matrices. These stress patterns themselves can orient the cell behaviours underlying morphogenesis. As a result of this interplay, tissue shape emerges in a mechanical process that tightly couples mechanics and genetics.
Language	English
Publishing date	2017-07
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1312473-0
ISSN	1096-3634 ; 1084-9521
ISSN (online)	1096-3634
ISSN	1084-9521
DOI	10.1016/j.semcdb.2017.04.004
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Article ; Online: Multiple roles for lipids in the Hedgehog signalling pathway.

Eaton, Suzanne

Nature reviews. Molecular cell biology

2008 Volume 9, Issue 6, Page(s) 437–445

Abstract: The identification of endogenous sterol derivatives that modulate the Hedgehog (Hh) signalling pathway has begun to suggest testable hypotheses for the cellular biological functions of Patched, and for the lipoprotein association of Hh. Progress in the ... ...

Abstract	The identification of endogenous sterol derivatives that modulate the Hedgehog (Hh) signalling pathway has begun to suggest testable hypotheses for the cellular biological functions of Patched, and for the lipoprotein association of Hh. Progress in the field of intracellular sterol trafficking has emphasized how tightly the distribution of intracellular sterol is controlled, and suggests that the synthesis of sterol derivatives can be influenced by specific sterol-delivery pathways. The combination of this field with Hh studies will rapidly give us a more sophisticated understanding of both the Hh signal-transduction pathway and the cell biology of sterol metabolism.
MeSH term(s)	Animals ; Hedgehog Proteins/chemistry ; Hedgehog Proteins/physiology ; Humans ; Lipids/chemistry ; Lipids/physiology ; Protein Transport/physiology ; Signal Transduction/physiology
Chemical Substances	Hedgehog Proteins ; Lipids
Language	English
Publishing date	2008-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2031313-5
ISSN	1471-0080 ; 1471-0072
ISSN (online)	1471-0080
ISSN	1471-0072
DOI	10.1038/nrm2414
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Zs.A 5446: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Retromer retrieves wntless.

Eaton, Suzanne

Developmental cell

2008 Volume 14, Issue 1, Page(s) 4–6

Abstract: Wntless is a sorting receptor required for Wnt secretion. Wntless is retrieved from endosomes to the Golgi by retromer, permitting Wntless reutilization in Wnt transport. In the absence of retromer, Wntless is degraded in lysosomes and Wnt secretion is ... ...

Abstract	Wntless is a sorting receptor required for Wnt secretion. Wntless is retrieved from endosomes to the Golgi by retromer, permitting Wntless reutilization in Wnt transport. In the absence of retromer, Wntless is degraded in lysosomes and Wnt secretion is impaired.
MeSH term(s)	Animals ; Endosomes/physiology ; Golgi Apparatus/physiology ; Models, Biological ; Signal Transduction/physiology ; Transport Vesicles/metabolism ; Vesicular Transport Proteins/metabolism ; Wnt Proteins/metabolism ; trans-Golgi Network/physiology
Chemical Substances	Vesicular Transport Proteins ; Wnt Proteins
Language	English
Publishing date	2008-01
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	2054967-2
ISSN	1878-1551 ; 1534-5807
ISSN (online)	1878-1551
ISSN	1534-5807
DOI	10.1016/j.devcel.2007.12.014
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Zs.A 5742: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Apico-basal cell compression regulates Lamin A/C levels in epithelial tissues.

Iyer, K Venkatesan / Taubenberger, Anna / Zeidan, Salma Ahmed / Dye, Natalie A / Eaton, Suzanne / Jülicher, Frank

Nature communications

2021 Volume 12, Issue 1, Page(s) 1756

Abstract: The levels of nuclear protein Lamin A/C are crucial for nuclear mechanotransduction. Lamin A/C levels are known to scale with tissue stiffness and extracellular matrix levels in mesenchymal tissues. But in epithelial tissues, where cells lack a strong ... ...

Abstract	The levels of nuclear protein Lamin A/C are crucial for nuclear mechanotransduction. Lamin A/C levels are known to scale with tissue stiffness and extracellular matrix levels in mesenchymal tissues. But in epithelial tissues, where cells lack a strong interaction with the extracellular matrix, it is unclear how Lamin A/C is regulated. Here, we show in epithelial tissues that Lamin A/C levels scale with apico-basal cell compression, independent of tissue stiffness. Using genetic perturbations in Drosophila epithelial tissues, we show that apico-basal cell compression regulates the levels of Lamin A/C by deforming the nucleus. Further, in mammalian epithelial cells, we show that nuclear deformation regulates Lamin A/C levels by modulating the levels of phosphorylation of Lamin A/C at Serine 22, a target for Lamin A/C degradation. Taken together, our results reveal a mechanism of Lamin A/C regulation which could provide key insights for understanding nuclear mechanotransduction in epithelial tissues.
MeSH term(s)	Animals ; Cell Line ; Cell Nucleus/physiology ; Dogs ; Drosophila ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Epithelium/metabolism ; Lamin Type A/genetics ; Lamin Type A/metabolism ; Lamins/genetics ; Lamins/metabolism ; Madin Darby Canine Kidney Cells ; Mechanotransduction, Cellular/physiology ; Phosphorylation ; Stress, Mechanical
Chemical Substances	Drosophila Proteins ; LamC protein, Drosophila ; Lamin Type A ; Lamins
Language	English
Publishing date	2021-03-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-22010-9
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Article ; Online: Hedgehog signaling can enhance glycolytic ATP production in the Drosophila wing disc.

Nellas, Ioannis / Iyer, K Venkatesan / Iglesias-Artola, Juan M / Pippel, Martin / Nadler, André / Eaton, Suzanne / Dye, Natalie A

EMBO reports

2022 Volume 23, Issue 11, Page(s) e54025

Abstract: Adenosine triphosphate (ATP) production and utilization is critically important for animal development. How these processes are regulated in space and time during tissue growth remains largely unclear. We used a FRET-based sensor to dynamically monitor ... ...

Abstract	Adenosine triphosphate (ATP) production and utilization is critically important for animal development. How these processes are regulated in space and time during tissue growth remains largely unclear. We used a FRET-based sensor to dynamically monitor ATP levels across a growing tissue, using the Drosophila larval wing disc. Although steady-state levels of ATP are spatially uniform across the wing pouch, inhibiting oxidative phosphorylation reveals spatial differences in metabolic behavior, whereby signaling centers at compartment boundaries produce more ATP from glycolysis than the rest of the tissue. Genetic perturbations indicate that the conserved Hedgehog signaling pathway can enhance ATP production by glycolysis. Collectively, our work suggests the existence of a homeostatic feedback loop between Hh signaling and glycolysis, advancing our understanding of the connection between conserved developmental patterning genes and ATP production during animal tissue development.
MeSH term(s)	Animals ; Drosophila/genetics ; Drosophila/metabolism ; Hedgehog Proteins/genetics ; Hedgehog Proteins/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Adenosine Triphosphate/metabolism ; Gene Expression Regulation, Developmental ; Wings, Animal/metabolism ; Glycolysis ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism
Chemical Substances	Hedgehog Proteins ; Drosophila Proteins ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2022-09-22
Publishing country	England
Document type	Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202154025
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Zs.A 5433: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Range of SHH signaling in adrenal gland is limited by membrane contact to cells with primary cilia.

Mateska, Ivona / Nanda, Kareena / Dye, Natalie A / Alexaki, Vasileia Ismini / Eaton, Suzanne

The Journal of cell biology

2020 Volume 219, Issue 12

Abstract: The signaling protein Sonic Hedgehog (SHH) is crucial for the development and function of many vertebrate tissues. It remains largely unclear, however, what defines the range and specificity of pathway activation. The adrenal gland represents a useful ... ...

Abstract	The signaling protein Sonic Hedgehog (SHH) is crucial for the development and function of many vertebrate tissues. It remains largely unclear, however, what defines the range and specificity of pathway activation. The adrenal gland represents a useful model to address this question, where the SHH pathway is activated in a very specific subset of cells lying near the SHH-producing cells, even though there is an abundance of lipoproteins that would allow SHH to travel and signal long-range. We determine that, whereas adrenal cells can secrete SHH on lipoproteins, this form of SHH is inactive due to the presence of cosecreted inhibitors, potentially explaining the absence of long-range signaling. Instead, we find that SHH-producing cells signal at short range via membrane-bound SHH, only to receiving cells with primary cilia. Finally, our data from NCI-H295R adrenocortical carcinoma cells suggest that adrenocortical tumors may evade these regulatory control mechanisms by acquiring the ability to activate SHH target genes in response to TGF-β.
MeSH term(s)	Adrenal Glands/metabolism ; Animals ; Cell Line, Tumor ; Cilia/genetics ; Cilia/metabolism ; Hedgehog Proteins/genetics ; Hedgehog Proteins/metabolism ; Lipoproteins/genetics ; Lipoproteins/metabolism ; Mice ; Mice, Transgenic ; Signal Transduction
Chemical Substances	Hedgehog Proteins ; Lipoproteins ; Shh protein, mouse
Language	English
Publishing date	2020-10-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218154-x
ISSN	1540-8140 ; 0021-9525
ISSN (online)	1540-8140
ISSN	0021-9525
DOI	10.1083/jcb.201910087
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Article ; Online: Cargo sorting in the endocytic pathway: a key regulator of cell polarity and tissue dynamics.

Eaton, Suzanne / Martin-Belmonte, Fernando

Cold Spring Harbor perspectives in biology

2014 Volume 6, Issue 10, Page(s) a016899

Abstract: The establishment and maintenance of polarized plasma membrane domains is essential for cellular function and proper development of organisms. Epithelial cells polarize along two fundamental axes, the apicobasal and the planar, both depending on finely ... ...

Abstract	The establishment and maintenance of polarized plasma membrane domains is essential for cellular function and proper development of organisms. Epithelial cells polarize along two fundamental axes, the apicobasal and the planar, both depending on finely regulated protein trafficking mechanisms. Newly synthesized proteins destined for either surface domain are processed along the biosynthetic pathway and segregated into distinct subsets of transport carriers emanating from the trans-Golgi network or endosomes. This exocytic trafficking has been identified as essential for proper epithelial polarization. Accumulating evidence now reveals that endocytosis and endocytic recycling play an equally important role in epithelial polarization and the appropriate localization of key polarity proteins. Here, we review recent work in metazoan systems illuminating the connections between endocytosis, postendocytic trafficking, and cell polarity, both apicobasal and planar, in the formation of differentiated epithelial cells, and how these processes regulate tissue dynamics.
MeSH term(s)	Animals ; Biological Transport ; Cell Differentiation ; Cell Polarity ; Endocytosis/physiology ; Epithelial Cells/cytology ; Epithelial Cells/metabolism ; Models, Biological
Language	English
Publishing date	2014-08-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a016899
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Article ; Online: Core PCP mutations affect short-time mechanical properties but not tissue morphogenesis in the

Piscitello-Gómez, Romina / Gruber, Franz S / Krishna, Abhijeet / Duclut, Charlie / Modes, Carl D / Popović, Marko / Jülicher, Frank / Dye, Natalie A / Eaton, Suzanne

eLife

2023 Volume 12

Abstract: How morphogenetic movements are robustly coordinated in space and time is a fundamental open question in biology. We study this question using the wing ... ...

Abstract	How morphogenetic movements are robustly coordinated in space and time is a fundamental open question in biology. We study this question using the wing of
MeSH term(s)	Animals ; Drosophila/metabolism ; Drosophila melanogaster/physiology ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Pupa/genetics ; Wings, Animal/physiology ; Morphogenesis/genetics ; Cell Polarity ; Mutation
Chemical Substances	Drosophila Proteins
Language	English
Publishing date	2023-12-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.85581
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