Cytoskeletal coordination and intercellular signalling during metazoan embryogenesis

Development ◽  
1981 ◽  
Vol 65 (1) ◽  
pp. 1-25
Author(s):  
J. B. Tucker
Keyword(s):  
Cell Surface ◽  
Spatial Organization ◽  
Positional Information ◽  
Animal Tissues ◽  
Marked Contrast ◽  
Cytoskeletal Organization ◽  
Motor Network ◽  
Intercellular Signalling ◽  
Signal Mode ◽  
Spatiotemporal Integration

This article draws attention to certain recently discovered features of cell surface organization and cytoskeletal deployment that may be revealing a new basis for intercellular signalling during metazoan embryogenesis. It is a signal mode that could coordinate many aspects of ‘Entwicklungsmechanik’ by spatiotemporal integration of the cytoskeletal/motor network throughout developing tissues. Evidence that this is achieved by ‘intercellular cytoskeletal/plasma membrane connecting systems’ which coordinate the spatial organization of microtubules, microfilaments, and intermediate filaments in developing animal tissues is critically examined. It is argued that this system does operate but that it is not used to transmit positional information in embryonic fields. However, it probably responds to such information and might play an important part in establishing field boundaries during the very earliest stages of embryogenesis. Certain aspects of cell surface organization in contemporary protozoans reveal ways in which the Protozoa could have been pre-adapted for the employment of cytoskeletal/cell surface signalling during the advent of multicellularity. In marked contrast, such signalling does not appear to be exploited during plant morphogenesis. The extent to which cytoskeletal organization might be coordinated in sisier cells by transmission of spatial instructions during cell division in both animal and plant tissues is also considered.

scholarly journals H3K9me2 orchestrates inheritance of spatial positioning of peripheral heterochromatin through mitosis

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Andrey Poleshko ◽  
Cheryl L Smith ◽  
Son C Nguyen ◽  
Priya Sivaramakrishnan ◽  
Karen G Wong ◽  
...  
Keyword(s):  
Cell Division ◽  
Spatial Organization ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Positional Information ◽  
Specific Gene ◽  
Cell Type ◽  
Histone 3 ◽  
Spatial Positioning ◽  
Peripheral Heterochromatin

Cell-type-specific 3D organization of the genome is unrecognizable during mitosis. It remains unclear how essential positional information is transmitted through cell division such that a daughter cell recapitulates the spatial genome organization of the parent. Lamina-associated domains (LADs) are regions of repressive heterochromatin positioned at the nuclear periphery that vary by cell type and contribute to cell-specific gene expression and identity. Here we show that histone 3 lysine 9 dimethylation (H3K9me2) is an evolutionarily conserved, specific mark of nuclear peripheral heterochromatin and that it is retained through mitosis. During mitosis, phosphorylation of histone 3 serine 10 temporarily shields the H3K9me2 mark allowing for dissociation of chromatin from the nuclear lamina. Using high-resolution 3D immuno-oligoFISH, we demonstrate that H3K9me2-enriched genomic regions, which are positioned at the nuclear lamina in interphase cells prior to mitosis, re-associate with the forming nuclear lamina before mitotic exit. The H3K9me2 modification of peripheral heterochromatin ensures that positional information is safeguarded through cell division such that individual LADs are re-established at the nuclear periphery in daughter nuclei. Thus, H3K9me2 acts as a 3D architectural mitotic guidepost. Our data establish a mechanism for epigenetic memory and inheritance of spatial organization of the genome.

Intercellular signalling in mesoderm formation during amphibian development

1993 ◽  
Vol 340 (1293) ◽  
pp. 287-296 ◽  
Keyword(s):  
Positional Information ◽  
Cell Types ◽  
The Body ◽  
Fibroblast Growth ◽  
Blastula Stage ◽  
Mesodermal Cell ◽  
Inductive Interaction ◽  
Mesoderm Formation ◽  
Stage Embryo ◽  
Intercellular Signalling

The mesoderm of amphibian embryos arises through an inductive interaction in which a signal from the vegetal hemisphere of the blastula-stage embryo acts on overlying equatorial cells. Strong candidates for endogenous mesoderm-inducing signals include members of the fibroblast growth factor (FGF) and activin families. In this paper we show that cells form different mesodermal cell types in response to different concentrations of these factors, and that graded distributions of activin and FGF can, in principle, provide sufficient positional information to generate the body plan of the Xenopus embryo.

scholarly journals H3K9me2 orchestrates inheritance of spatial positioning of peripheral heterochromatin through mitosis

2019 ◽  
Author(s):  
Andrey Poleshko ◽  
Cheryl L. Smith ◽  
Son C. Nguyen ◽  
Priya Sivaramakrishnan ◽  
John Isaac Murray ◽  
...  
Keyword(s):  
Cell Division ◽  
Spatial Organization ◽  
Nuclear Periphery ◽  
Nuclear Lamina ◽  
Positional Information ◽  
Specific Gene ◽  
Cell Type ◽  
Histone 3 ◽  
Spatial Positioning ◽  
Peripheral Heterochromatin

AbstractCell-type-specific 3D organization of the genome is unrecognizable during mitosis. It remains unclear how essential positional information is transmitted through cell division such that a daughter cell recapitulates the spatial genome organization of the parent. Lamina-associated domains (LADs) are regions of repressive heterochromatin positioned at the nuclear periphery that vary by cell type and contribute to cell-specific gene expression and identity. Here we show that histone 3 lysine 9 dimethylation (H3K9me2) is an evolutionarily conserved, specific mark of nuclear peripheral heterochromatin and that it is retained through mitosis. During mitosis, phosphorylation of histone 3 serine 10 temporarily shields the H3K9me2 mark allowing for dissociation of chromatin from the nuclear lamina. Using high-resolution 3D immuno-oligoFISH, we demonstrate that H3K9me2-enriched genomic regions, which are positioned at the nuclear lamina in interphase cells prior to mitosis, re-associate with the forming nuclear lamina before mitotic exit. The H3K9me2 modification of peripheral heterochromatin ensures that positional information is safeguarded through cell division such that individual LADs are re-established at the nuclear periphery in daughter nuclei. Thus, H3K9me2 acts as a 3D architectural mitotic guidepost. Our data establish a mechanism for epigenetic memory and inheritance of spatial organization of the genome.

Studies of early stages of differentiation of the cellular slime mould Dictyostelium discoideum

Development ◽  
1982 ◽  
Vol 67 (1) ◽  
pp. 181-193
Author(s):  
P. T. Sharpe ◽  
T. E. Treffry ◽  
D. J. Watts
Keyword(s):  
Cell Differentiation ◽  
Cell Surface ◽  
Surface Properties ◽  
Dictyostelium Discoideum ◽  
Axenic Culture ◽  
Surface Heterogeneity ◽  
Positional Information ◽  
Phase System ◽  
Two Phase ◽  
Cell Surface Properties

Countercurrent distribution in a polymer, two-phase system has been used to study changes in the cell surface properties of amoebae of Dictyostelium discoideum. Amoebae harvested during exponential growth in axenic culture and during the subsequent first six hours of development on Millipore filters were distributed as a single peak. However, the position of the peak changed during the period of early development which showed that changes in cell surface properties were occurring. At aggregation (8 h), the peak markedly broadened, indicating considerable increase in cell surface heterogeneity amongst the amoebae, and heterogeneity was so great by 9–10 h that the amoebae distributed as two peaks. Amoebae from one peak were shown to be precursors of spores while amoebae from the other peak appeared to be precursors of stalk cells. Similarly, amoebae from the trailing and leading edges of the broad peak, formed from amoebae beginning to aggregate (8 h), were found to have different fates. Thus cell differentiation had been found at times of development prior to formation of aggregates having apical tips or anterior-posterior polarity and neither of these features of aggregates can be essential for initiation of cell differentiation. It is therefore concluded that differentiation is not initiated in D. discoideum in response to ‘positional information’.

Studies of nuclear and cytoplasmic behaviour during the five mitotic cycles that precede gastrulation in Drosophila embryogenesis

1983 ◽  
Vol 61 (1) ◽  
pp. 31-70 ◽  
Author(s):  
V.E. Foe ◽  
B.M. Alberts
Keyword(s):  
Average Duration ◽  
Morphological Changes ◽  
Positional Information ◽  
Cytoskeletal Organization ◽  
The Core ◽  
Drosophila Embryogenesis ◽  
Nuclear Cycle ◽  
Frozen Embryos ◽  
Specific Manner ◽  
Peripheral Cytoplasm

Using differential interference contrast optics, combined with cinematography, we have studied the morphological changes that the living, syncytial embryo undergoes from stage 10 through 14 of Drosophila embryogenesis, that is just prior to and during formation of the cellular blastoderm. We have supplemented these studies with data collected from fixed, stained, whole embryos. The following information has been obtained. The average duration of nuclear cycles 10, 11, 12 and 13 is about 9, 10, 12 and 21 min, respectively (25 degrees C). In these four cycles, the duration of that portion of the mitotic period that lacks a discrete nuclear envelope is 3, 3, 3 and 5 min, respectively. The length of nuclear cycle 14 varies in a position-specific manner throughout the embryo, the shortest cycles being of 65 min duration. During nuclear cycles 10 through 13, it is commonly observed in living embryos that the syncytial blastoderm nuclei enter (and leave) mitosis in one of two waves that originate nearly simultaneously from the opposite anterior and posterior poles of the embryo, and terminate in its midregion. From our preparations of quick-frozen embryos, we estimate that these mitotic waves take on average about half a minute to travel over the embryonic surface from pole to equator. The yolk nuclei, which remain in the core of the embryo when the rest of the nuclei migrate to the periphery, divide in synchrony with the migrating nuclei at nuclear cycles 8 and 9, and just after the now peripherally located nuclei at nuclear cycle 10. After cycle 10, these yolk nuclei cease dividing and become polyploid. The syncytial embryo has at least three distinct levels of cytoskeletal organization: structured domains of cytoplasm are organized around each blastoderm nucleus; radially directed tracks orient colchicine-sensitive saltatory transport throughout the peripheral cytoplasm; and a long-range organization of the core of the embryo makes possible coherent movements of the large inner yolk mass in concert with each nuclear cycle. This highly organized cytoplasm may be involved in providing positional information for the important process of nuclear determination that is known to occur during these stages.

scholarly journals The Tetraspan Molecule Cd151, a Novel Constituent of Hemidesmosomes, Associates with the Integrin α6β4 and May Regulate the Spatial Organization of Hemidesmosomes

2000 ◽  
Vol 149 (4) ◽  
pp. 969-982 ◽  
Author(s):  
Lotus M.Th. Sterk ◽  
Cecile A.W. Geuijen ◽  
Lauran C.J.M. Oomen ◽  
Jero Calafat ◽  
Hans Janssen ◽  
...  
Keyword(s):  
Cell Surface ◽  
Spatial Organization ◽  
Transmembrane Domain ◽  
Focal Adhesions ◽  
Surface Protein ◽  
K562 Cells ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Junctional Epidermolysis Bullosa ◽  
Integrin Α6β4

CD151 is a cell surface protein that belongs to the tetraspan superfamily. It associates with other tetraspan molecules and certain integrins to form large complexes at the cell surface. CD151 is expressed by a variety of epithelia and mesenchymal cells. We demonstrate here that in human skin CD151 is codistributed with α3β1 and α6β4 at the basolateral surface of basal keratinocytes. Immunoelectron microscopy showed that CD151 is concentrated in hemidesmosomes. By immunoprecipitation from transfected K562 cells, we established that CD151 associates with α3β1 and α6β4. In β4-deficient pyloric atresia associated with junctional epidermolysis bullosa (PA-JEB) keratinocytes, CD151 and α3β1 are clustered together at the basal cell surface in association with patches of laminin-5. Focal adhesions are present at the periphery of these clusters, connected with actin filaments, and they contain both CD151 and α3β1. Transient transfection studies of PA-JEB cells with β4 revealed that the integrin α6β4 becomes incorporated into the α3β1-CD151 clusters where it induces the formation of hemidesmosomes. As a result, the amount of α3β1 in the clusters diminishes and the protein becomes restricted to the peripheral focal adhesions. Furthermore, CD151 becomes predominantly associated with α6β4 in hemidesmosomes, whereas its codistribution with α3β1 in focal adhesions becomes partial. The localization of α6β4 in the pre-hemidesmosomal clusters is accompanied by a strong upregulation of CD151, which is at least partly due to increased cell surface expression. Using β4 chimeras containing the extracellular and transmembrane domain of the IL-2 receptor and the cytoplasmic domain of β4, we found that for recruitment of CD151 into hemidesmosomes, the β4 subunit must be associated with α6, confirming that integrins associate with tetraspans via their α subunits. CD151 is the only tetraspan identified in hemidesmosomal structures. Others, such as CD9 and CD81, remain diffusely distributed at the cell surface. In conclusion, we show that CD151 is a major component of (pre)-hemidesmosomal structures and that its recruitment into hemidesmosomes is regulated by the integrin α6β4. We suggest that CD151 plays a role in the formation and stability of hemidesmosomes by providing a framework for the spatial organization of the different hemidesmosomal components.

scholarly journals Discrete spatial organization of TGFβ receptors couples receptor multimerization and signaling to cellular tension

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Joanna P Rys ◽  
Christopher C DuFort ◽  
David A Monteiro ◽  
Michelle A Baird ◽  
Juan A Oses-Prieto ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cellular Response ◽  
Spatial Organization ◽  
Focal Adhesions ◽  
Single Particle Tracking ◽  
Cell Surface Receptors ◽  
Surface Receptors ◽  
Tgfβ Receptors ◽  
Physical Cues ◽  
Tgfβ Receptor

Cell surface receptors are central to the cell's ability to generate coordinated responses to the multitude of biochemical and physical cues in the microenvironment. However, the mechanisms by which receptors enable this concerted cellular response remain unclear. To investigate the effect of cellular tension on cell surface receptors, we combined novel high-resolution imaging and single particle tracking with established biochemical assays to examine TGFβ signaling. We find that TGFβ receptors are discretely organized to segregated spatial domains at the cell surface. Integrin-rich focal adhesions organize TβRII around TβRI, limiting the integration of TβRII while sequestering TβRI at these sites. Disruption of cellular tension leads to a collapse of this spatial organization and drives formation of heteromeric TβRI/TβRII complexes and Smad activation. This work details a novel mechanism by which cellular tension regulates TGFβ receptor organization, multimerization, and function, providing new insight into the mechanisms that integrate biochemical and physical cues.

scholarly journals Studies on the function of cell surface glycoproteins. II. Possible role of surface glycoproteins in the control of cytoskeletal organization and surface morphology.

1979 ◽  
Vol 80 (2) ◽  
pp. 403-415 ◽  
Author(s):  
C H Damsky ◽  
D E Wylie ◽  
C A Buck
Keyword(s):  
Cell Surface ◽  
Surface Morphology ◽  
Specific Interaction ◽  
Cytoskeletal Organization ◽  
Fundamental Part ◽  
Transmission Electron ◽  
Radioimmune Assay ◽  
Cell Surface Morphology ◽  
Surface Glycoproteins

Immunoglobulin from goat antiserum directed against purified surface membranes from transformed BHK21/C13 cells (anti-M) has been shown to cause both control and transformed hamster cells to round and detach from the substrate (see accompanying paper). This paper documents the effects of the antiserum on the cytoskeletal organization and cell surface morphology of control BHK21/C13 cells examined by scanning and transmission electron microscopy. As a result of antiserum-induced rounding, the normally smooth cell surface becomes covered with filopodia and blebs, and the organization of all three components of the filamentous cytoskeleton is altered. In terms of cell surface morphology and cytoskeletal organization, the cells resemble rounded, postmitotic or trypsinized BHK cells rather than cells treated with either anticytoskeletal drugs or lectins. Immunocytochemical and radioimmune assay experiments support the suggestion that the rounding reaction induced by anti-M serum results from the specific interaction of antibodies with molecules on the cell surface. It is suggested that anti-M serum induces alterations in cytoskeletal organization via a transmembrane signal and that cytoskeletal reorganization is a fundamental part of the rounding and detachment process.

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