|
|
|
Expr4504
|
MRG-1 is highly enriched in nuclei and concentrated on chromatin. In early embryos, MRG-1 is present in the nuclei of all blastomeres. In late embryos and young larvae, MRG-1 staining is higher in the nuclei of the two primordial germ cells, Z2 and Z3, than in somatic blastomeres. In larvae and adults, MRG-1 staining is seen primarily in the nuclei of germ cells, although it is also faintly visible in the nuclei of several somatic cell types, including intestinal cells. In the adult germ line, all germ nuclei in the mitotic and meiotic regions are stained. These results demonstrate that MRG-1 is present in the germ line at all stages of development and is maternally loaded into embryos. In addition, zygotically expressed MRG-1 is produced in all cells by at least the 100-cell stage; it accumulates to higher levels in the primordial germ cells than in somatic tissues. |
Expressed in nuclei. |
|
|
|
Expr15550
|
Both SLD-3 and SLD-2 showed asymmetric localisation, with more protein in the AB cell nucleus, than P1. This asymmetry was not limited to the MosSCI alleles, as we obtained a similar result using immuno-fluorescence of endogenous SLD-2. Asymmetric and asynchronous divisions continue beyond the two-cell stage, with the descendants of the AB cell (ABa and ABp) having shorter cell cycles than the descendants of the P1 cell (EMS and P2) with P2 having the longest S-phase of these cells. We analysed the abundance of SLD-2 and SLD-3 in 4-cell stage embryos and these two proteins remained asymmetric at this stage with EMS and P2 having significantly less protein than the AB cell lineage. SLD-2 abundance was also significantly lower in the P2 cell than the EMS cell. |
|
|
INX-3 detected during very early stages of development is likely to be maternally derived, since INX-3::GFP expressed zygotically is first detected by anti-GFP antibodies at approximately the 28-cell stage. |
|
Expr2546
|
At the late first larval (L1) stage, INX-3 is present transiently in some newly generated cells. The postembryonic motor neurons, descendants of the Pn.a cells, express INX-3 briefly. INX-3 is also detected briefly in cells of the first two divisions of the M blast cell, coelomocytes, and sex muscles. By the comma stage, corresponding to early embryonic morphogenesis, INX-3 is still broadly expressed, but the pattern of expression becomes more restricted as morphogenesis proceeds. Because INX-3 is localized principally in puncta at plasma membranes, it is hard to assign expression unambiguously to individual cells; however, expression in major cell types or organs is clear. Double-labeling embryos with anti-INX-3 and MH27, a mAb that binds AJM-1 in apical epithelial intercellular junctions, indicated that, at the comma stage, INX-3 is localized to the developing intestine, pharynx, and hypodermis (epidermis), at minimum. During late morphogenesis, from the 3-fold stage until hatching, INX-3 is found principally in the posterior pharynx (isthmus and terminal bulb), at the anteriormost tip of the pharynx, in the region of the posterior intestine (probably intestinal muscles or rectal cells) and in the hypodermis. Expression in these tissues continues throughout development into adulthood with the exception of the hypodermis. Hypodermal expression is strong at the time of hatching, and INX-3 is present in plaques at the intercellular boundaries between most hypodermal cells except at the ventral midline between paired P cells; however, INX-3 becomes undetectable in the hypodermis shortly after hatching. INX-3 protein is first detected at the embryonic 2-cell stage. It is localized to small plaques at cellcell interfaces and can be detected throughout early embryogenesis in a pattern suggesting that most or all cells express inx-3. In adults, INX-3 is reduced such that only a few plaques are associated with vulval muscles. In the late L3 stage, INX-3 expression begins in the sex myoblasts (SMs). Expression continues in SM descendants so that all 16 sex muscles stain with anti-INX-3 in early L4 animals, confirming results obtained with an inx-3::gfp translational fusion gene. |
At embryonic 2-cell stage, localized to small plaques at cellcell interfaces. At the late first larval (L1) stage, INX-3 is present transiently in some newly generated cells, and in cells of the first two divisions of the M blast cell, coelomocytes, and sex muscles. INX-3 is readily detectable in the cytoplasm of these cells, as well as in cell-surface plaques. By the comma stage, INX-3 is localized principally in puncta at plasma membranes. At comma stage, within intestinal cells, whose large size allows easy visualization of subcellular location, INX-3 is localized to the basal portion of lateral membranes. |
|
|
|
Expr14682
|
We first show the localization of UNC-59 at the cleavage furrow (previously shown with antibody staining, (Nguyen et al. 2000)) during a time lapse of cell divisions in early 2- to 4-cell stages of embryogenesis and throughout embryogenesis (cleavage rings in older embryos. Septins are also important for gonad morphogenesis and distal tip cell (DTC) migration (Nguyen et al. 2000) where UNC-59 protein is detected throughout gonad development in the rachis (previously shown with endogenously tagged unc-59::mKate, (Priti et al. 2018)) and DTCs. We highlight UNC-59/Septin localization in the DTC (previously shown with a transgene, (Finger et al. 2003)) at the L2 and L3 stages where it is organized into bundles (DeMay et al. 2011) and ring structures. The two bilateral sex myoblast cells express UNC-59 during their posterior to anterior migration in the L2 and early L3 stage and continue to express UNC-59 in these cells as they differentiate into vulval muscles in the late L3 to early L4 stages. Lastly, we show UNC-59/Septin expression and localization in tissue not previously reported: in the pharynx (cells of the buccal cavity, anterior procorpus, and terminal bulb); in the seam cells, both in bundles and at the cleavage furrows, beginning in the L1 stage and continuing throughout development and into the adult; and in sperm surrounding an embryo that has exited the spermatheca. |
|
|
early embryo (author) = blastula embryo (curator) --wjc. |
|
Expr1736
|
In early embryos, MES-3 protein is present in the nuclei of all cells. As embryogenesis progresses, staining gradually diminishes in somatic cells. In late embryos and L1 larvae, MES-3 is detectable in some somatic cells but is most prominent in Z2 and Z3, the primordial germ cells. The nuclear staining of MES-3 is reduced below detection in any of the four nonconditional alleles of mes-3. In wild type adults, MES-3 is most prominent in germline nuclei and is occasionally barely detectable in intestinal nuclei. In the germline, it is present at low levels in distal mitotic nuclei, undetectable in the pachytene region of the distal arm, and present at elevated levels in the proximal meiotic region and in oocytes. |
MES-3 is localized predominantly in nuclei. The immunolocalization pattern of MES-3 was analyzed in embryos, using confocal microscopy. Cells at different stages of mitosis were stained by affinity-purified anti-MES-3 antibody and anti-penta-acetylated H4 antibody to visualize chromosomes. During interphase and prometaphase, when condensed chromosomes are clearly visible in nuclei, MES-3 protein is not obviously concentrated on chromosomes; instead it appears evenly distributed in the nucleoplasm. During metaphase and early anaphase, when nuclear envelopes are broken down, some MES-3 protein is detectably associated with chromosomes. |
|
This information was extracted from published material (Archana Sharma-Oates, Andrew Mounsey and Ian A. Hope). |
|
Expr677
|
At one cell stage, there is no signal detected. Expression is first detected at two and four cell stage, pattern is variable at this stage. In most (35/48) of four cell embryos transcript is detected in posterior P1 cell or its immediate daughters. By 8 cell stage, signal detected in all blastomeres. In 3/48 expression is seen in the somatic AB cell and its immediate daughters, whereas 10/48 embryos ftt-2 messages were present in both lineages. ftt-2 transcript levels remain high in older embryos and during early elongation stage of morphogenesis, the transcript becomes localized to the region of the developing gonad and gut. Undetectable in maturing germ cells or maturing oocytes. |
|
|
|
|
Expr2579
|
SCC-1/COH-2 was expressed in germ cells throughout the development, including the adult stage. SCC-1/COH-2 was detected in virtually all mitotic germ nuclei. Similarly to somatic cells in embryos, SCC-1/COH-2 was dispersed in the cytoplasm at mitotic prometaphase and was absent from the condensed anaphase chromosomes in germ cells. In female germ cells that entered meiotic prophase in adult hermaphrodites, SCC-1/COH-2 was observed uniformly in the nuclei. It was unclear whether SCC-1/COH-2 localized to the condensed meiotic chromosomes, because of the strong SCC-1/COH-2 signal emitted from the nucleoplasm. SCC-1/COH-2 was detected also in male germ cells at mitosis and meiosis, but it was not detectable in mature sperm. SCC-1/COH-2 was strongly expressed in virtually all cells in early embryos, but its expression was gradually weakened, and the signal could hardly be detected in late embryos, in which cell division was ceased almost completely. Strong nuclear signals of SCC-1/COH-2 reappeared in larvae, though they were limited to a subset of cells. SCC-1/COH-2 was detectable only in cells that were going to divide. For example, in an L1 larva, intense SCC-1/COH-2 signals were detected in the 14 hypodermal V lineage cells, which divide synchronously. The SCC-1/COH-2 signal was dispersed and not detectable on condensed chromosomes, as observed in embryos of an intermediate stage. In a slightly older L1 larva, expression of SCC-1/COH-2 was seen in 22 P lineage cells to constitute the ventral nerve cord and in four Q lineage cells to produce posterior neuronal cells, all of which divide at the same time. In this L1 larva, no signal was detected in the V lineage cells, suggesting that the SCC-1/COH-2 protein is present only for a short time in the cell cycle, and likely to be degraded quickly after cell division. Larvae of later stages also expressed SCC-1/COH-2 in dividing cells: in an L3 larva, SCC-1/COH-2 was detected in four M lineage cells to produce the uterine and vulval muscle cells and in 10 P lineage vulval precursor cells, which divide concurrently. The embryos were stained with both anti-SCC-1/COH-2 antibodies and an antibody against a component of the nuclear pore complexes. The SCC-1/COH-2 signal was evenly distributed within the nuclear envelope except for the chromosomal region, suggesting that SCC-1/COH-2 molecules dissociated from the chromosomes at metaphase were trapped by the nuclear envelope. Consistently with this interpretation, the SCC-1/COH-2 staining around the metaphase plate was no longer seen at later stages of embryogenesis involving >30 cells, where nuclear envelope is known to break down before metaphase. SCC-1/COH-2 was dispersed into the whole cytoplasm of metaphase cells at these stages. |
SCC-1/COH-2 seemed to localize to the chromosomes in a cell cycle-dependent manner. In interphase, SCC-1/COH-2 was seen throughout the nucleus, overlapping largely with DNA. At mitotic prophase, SCC-1/COH-2 started to separate from condensing chromosomes, and it was not detected on the chromosomes at prometaphase and metaphase. At metaphase, the SCC-1/COH-2 signal seemed as if surrounding the metaphase plate, although it was possible that a small amount of SCC-1/COH-2 was remaining on the metaphase chromosomes but escaped detection, because cohesin is reported to become detectable on metaphase chromosomes only after detergent extraction of soluble background in other metazoans. The SCC-1/COH-2 signal was then dispersed in the cytoplasm at anaphase. At telophase, the SCC-1/COH-2 protein began to reaccumulate on the chromosomes. |
|
Picture: Fig. 5. The same pattern was seen with two separate antibodies raised against distinct PLP-1 peptides, and both nuclear and P granule expression was largely eliminated in plp-1 (RNAi) embryos, confirming their specificity. |
|
Expr8706
|
Immunoreactive PLP-1 localizes to the nuclei of all blastomeres beginning by the two-cell stage of embryogenesis, implying that PLP-1 is a maternally encoded transcription factor. It is also present in the germline-specific P granules of early embryos. |
PLP-1 is transiently asymmetrically localized during telophase of the dividing EMS cell (observed in 12 embryos at the correct stage), with higher levels of the protein in the chromatin of the future E cell nucleus and low or undetectable levels in that of MS. A similar transient asymmetry in PLP-1 levels was observed at many divisions throughout early development, starting at cleavage of the zygote, with higher levels seen in the cytoplasm and forming nucleus of the posterior daughter, P1 (observed in 5 embryos). The anteroposterior asymmetry in PLP-1 was also observed in the AB lineage during the division of the AB granddaughters (observed in 7 embryos): for example, PLP-1 is higher in the chromatin of the posterior daughter ABalp than that of its anterior sister ABala. In all cases, the asymmetry was observed only during telophase and at the time that nuclei were reassembling after cell division; the staining was symmetric at all other times. PLP-1 was always seen at higher levels in the forming nuclei of the posterior daughters. |
|
Other strain-- UL123 |
|
Expr103
|
This strain exhibits strong expression in the embryo. Expression is first seen in the 50-80 cell embryo and extends through to adulthood. It appears that most of the AB cells in the embryo stain, and what appears to be the cells of the C lineage. Some embryos exhibit staining in the two rows of nuclei that are the E lineage. All embryonic staining is very intense, and it spreads to the cytoplasm giving blue embryos, therefore obscuring the DAPI staining, making it difficult to count the number of cells in the embryos as each component begins expressing. This intense staining fades as the embryo ages, sometimes leaving blue comma stage embryos with no distinct nuclei staining. Hypodermal expression is seen in the 3 fold stage of embryogenesis and in young larvae which most probably are C-derived hyp-7 nuclei. Expression weakens as the worm gets older and is much less frequently expressed in adults. Some adults do show staining in the anterior hypodermal nuclei (hyp-3, hyp-4) and in the anterior hypodermal seam cells, also some nuclei stain in the tail. |
|
|
early embryo(author) = blastula embryo(curator). |
|
Expr584
|
gld-1 mRNA is contained in all blastmeres of embryos with 8 or fewer cells. Subsequently, gld-1 mRNA disappears rapidly from somatic blastmeres and is only detected in the germ lineage. By the 16 cell stage, gld-1 mRNA is only detected in P3. |
|
|
|
|
Expr2551
|
In situ hybridization analysis revealed that spn-4 mRNA was abundant in early embryos. The mRNA was present at the same level in all blastomeres up to the 4-cell stage. Afterwards, it persists in the P blastomere and its sister, and then just the germ lineage. The mRNA was also present in the adult gonads. |
|
|
|
|
Expr2947
|
In late embryos (after the comma stage) matefin staining decreased in all somatic cells but intensified in the nuclear envelopes of the two primordial germ cells, Z2 and Z3. The identity of Z2 and Z3 cells was verified by double labeling with antibodies against PGL-1, which is specific to germ cells. Throughout larva stages L1-L4 and in adults, matefin was present only in germ cells. Matefin signal declined during spermatogenesis and was undetectable in sperm. |
Matefin was detected at the nuclear envelope of all early embryonic cells. |
|
early embryo(author) = blastula embryo(curator). |
|
Expr572
|
SKN-1 protein first becomes visible in oocyte and sperm pronuclei before the first mitotic division of the zygote. SKN-1 becomes cytoplasmic as AB and P1 enter mitosis. P2 and EMS have more SKN-1 than AB daughters. By the 8-cell stage, the granddaughters of AB do not stain for SKN-1, but P1 granddaughters do. SKN-1 is not detectable by the 12-cell stage. |
After the first cleavage, SKN-1 protein locates at the nuclei of AB and P1. As AB and P1 enter mitosis, SKN-1 protein is distributed throughout cytoplasm. |
|
This information was extracted from published material (Archana Sharma-Oates, Andrew Mounsey and Ian A. Hope). |
|
Expr706
|
NHR-2 is detected in the nuclei of embryos as early as 2-cell stage. The protein is present in every nucleus until the 16-20 cell stage then no longer detected in germline precursor P4 and its sister D but at this point expression in other cells increase. No staining during or just after mitosis. 28-cell stage: Staining in E and MS descendants, variable expression generally weak particularly in E cells. Staining in ABplp and ABpr descendants also variable but can be quite strong. The other 10 AB cells and 4 C cells exhibit reproducible strong expression. 51-cell stage: No expression in descendants of E. Staining in C cells, many AB cells and some MS cells (particularly those in anterior and dorsal positions). As embryogenesis progresses NHR-2 expression is restricted to anterior and dorsal regions of embryo. 250 cell stage: Nuclei staining include (but not limited to) Cp descendants contributing to hyp7 synctium, many but not all AB descendants. NHR-2 last detected in one or a few nuclei in vicinity of excretory cell before expression ceases at early comma stage. |
|
|
See Expression pattern 546 for distribution of APX-1 protein. early embryo(author) = blastula embryo(curator). |
|
Expr545
|
Between the newly-fertilized 1-cell stage and the 8-cell stage, apx-1 mRNA is present in all blastomeres at equivalent levels. After the 8-cell stage, apx-1 mRNA rapidly disappears from somatic blastomeres; in 12-cell stage embryos, apx-1 mRNA is visible in the P3 blastomere, but disappears from MS and all other blastomeres. In the 36-cell stage and later embryos, apx-1 mRNA was detected in one to five unidentified nuclei. |
|
|
|
|
Expr2575
|
In situ hybridization analysis revealed that spn-4 mRNA was abundant in early embryos. The mRNA was present at the same level in all blastomeres up to the 4-cell stage. Afterwards, it persists in the P blastomere and its sister, and then just the germ lineage. The mRNA was also present in the adult gonads. |
|
|
|
|
Expr12428
|
NEG-1::GFP is asymmetrically localized in the early embryo. NEG-1::GFP was detected in the zygotic nucleus and at equal levels in both nuclei of the two-cell embryo (23 of 23). However, at the four-cell stage, NEG-1::GFP expression was markedly higher in nuclei of the anterior AB blastomeres than in the nuclei of EMS and P2 (31 of 34). Following the four-cell stage, NEG-1::GFP remained high in the granddaughters of the AB blastomere and diminished progressively in subsequent divisions (data not shown). In the adult germline, NEG- 1::GFP was observed in the nuclei of distal germ cells and the nuclei of growing oocytes except for the most proximal oocyte. Moreover, intense sub-nuclear localization of NEG-1:GFP was observed on condensed chromatin. |
|
|
Clone = pUL#PB45 Other strain-- UL457 Strain = UL411 |
|
Expr2117
|
Expression is confined to the embryo, and consists of two components. In pre-comma stage embryos strong expression is seen in a number of anteriorly located cells. These cells are possibly descendants of ABa. In 3-fold embryos a distinct component consists of expression in the hypodermal seam cells. This gene has homology to aldehyde dehydrogenases. |
|
|
Removing the coding region, and using only the Bluescript vector as a probe, does not show staining except a little background. As a negative control, the dpy-20 probe was used for RNA in situ hybridization and no staining in embryos was detected. |
|
Expr1099
|
1-cell, 2-cell and 4-cell embryos show uniform expression pattern. Expression in later embryos and young larvae is predominant in the head region. |
|
|
Subcellular localization: GLP-1 was found in the cytoplasm at the 2-cell stage, then in cytoplasm and membranes at 4-cell and 8-cell stages. Cytoplasmic GLP-1 fades after the 8-cell stage, and disappears by the 28-cell stage. Membrane-associated GLP-1 is faint by the 28-cell stage. The glp-1 mRNA was distributed uniformly through the 8-cell stage. Levels of glp-1 mRNA decline after the 8-cell stage and largely disappear by the 28-cell stage, though signal consistently persisted later in posterior parts of embryos. mRNA reappears after 100-cell stage, paralleling immunostaining results. early embryo(author) = blastula + gastrulating embryo(curator). |
|
Expr541
|
Faint expression in AB at 2-cell stage, becoming stronger in AB descendants after 4-cell stage. Signal weakens, between the 8- and 28-cell stages. GLP-1 not detected again until after the 100-cell stage in unidentified cells. |
GLP-1 was found in the cytoplasm at the 2-cell stage, then in cytoplasm and membranes at 4-cell and 8-cell stages. Cytoplasmic GLP-1 fades after the 8-cell stage, and disappears by the 28-cell stage. Membrane-associated GLP-1 is faint by the 28-cell stage. The glp-1 mRNA was distributed uniformly through the 8-cell stage. Levels of glp-1 mRNA decline after the 8-cell stage and largely disappear by the 28-cell stage, though signal consistently persisted later in posterior parts of embryos. mRNA reappears after 100-cell stage, paralleling immunostaining results. |
|
|
|
Expr15548
|
Both SLD-3 and SLD-2 showed asymmetric localisation, with more protein in the AB cell nucleus, than P1. This asymmetry was not limited to the MosSCI alleles, as we obtained a similar result using immuno-fluorescence of endogenous SLD-2. Asymmetric and asynchronous divisions continue beyond the two-cell stage, with the descendants of the AB cell (ABa and ABp) having shorter cell cycles than the descendants of the P1 cell (EMS and P2) with P2 having the longest S-phase of these cells. We analysed the abundance of SLD-2 and SLD-3 in 4-cell stage embryos and these two proteins remained asymmetric at this stage with EMS and P2 having significantly less protein than the AB cell lineage. SLD-2 abundance was also significantly lower in the P2 cell than the EMS cell. |
|
|
|
|
Expr15549
|
Both SLD-3 and SLD-2 showed asymmetric localisation, with more protein in the AB cell nucleus, than P1. This asymmetry was not limited to the MosSCI alleles, as we obtained a similar result using immuno-fluorescence of endogenous SLD-2. Asymmetric and asynchronous divisions continue beyond the two-cell stage, with the descendants of the AB cell (ABa and ABp) having shorter cell cycles than the descendants of the P1 cell (EMS and P2) with P2 having the longest S-phase of these cells. We analysed the abundance of SLD-2 and SLD-3 in 4-cell stage embryos and these two proteins remained asymmetric at this stage with EMS and P2 having significantly less protein than the AB cell lineage. SLD-2 abundance was also significantly lower in the P2 cell than the EMS cell. |
|
|
|
|
Expr2582
|
|
The OMA-1::GFP fluorescence in the developing oocytes and one-cell embryos recapitulated the wild-type spatial and temporal patterns of OMA-1 antibody staining. The punctate staining appeared more pronounced and resembled the characteristic pattern of germline P granules. Starting with the onset of the first mitotic division, the intensity of OMA-1-GFP fluorescence rapidly decreased, and by the time the division was complete, only approximately 10% remained. Interestingly, that remaining 10% of the GFP signal in the two-cell embryo was predominantly found in the germline precursor, P1, associated with what appeared to be P granules. The GFP signal continued to decrease in two-cell embryos and again was asymmetric after the next division, with most of the remaining fluorescence segregated to P2, where it was also predominantly associated with granules. The OMA-1-GFP signal became too weak to detect in the embryo after the four-cell stage. |
|
The strain, a pes-10::lacZ integrant, contained multiple copies of the transgene. |
|
Expr586
|
Expressed in somatic blastomeres. First seen in AB.a and AB.p at the 3-cell stage. Shortly after P1 divides, the mRNA appears in EMS. See Expression pattern 565 for expression at later embryonic stages. |
|
|
No detailed description for cellular expression pattern at later developmental stages. |
|
Expr1294
|
Expression scored from zygote til 50 cell embryo |
Antibody staining is detectable throughout the cytoplasm and at the periphery of blastomeres up to about the 50-cell stage. The peripheral staining is asymmetric in the cells of the germline lineage P0, P1, P2 and P3. Asymmetric peripheral localization of PAR-6 develops as the newly fertilized egg, P0, progresses through the cell cycle. Localized antibody staining is not detectable in unfertilized mature oocytes, nor in newly fertilized eggs undergoing the first meiotic division. Patchy PAR-6 staining was first detected at the periphery of the embryo after completion of meiosis I, as determined by the presence of a single polar body. 70% of embryos in meiosis II exhibit patchy PAR-6 staining all around the periphery with no obvious asymmetry (n=20). When the female pronucleus completes metaphase II as indicated by the presence of a second polar body, peripheral PAR-6 is restricted to the anterior 85% of embryo length. In embryos between prophase and telophase of the first mitosis, the peripheral PAR-6 is restricted to the anterior 55% EL of the embryos (n=24). During the first cleavage PAR-6 staining is detectable in the advancing furrow. Asymmetry of PAR-6 is also observed in P1 and P2, the germline cells in 2-cell and 4-cell embryos, respectively. Just after the first cleavage, strong peripheral staining is present where P1 apposes AB. The strength of this signal suggests that protein is present along this boundary in both cells. As the P1 cell progressed into prophase, PAR-6 distribution extends posteriorly, covering the anterior 30% of 13 of 16 P1 cells scored. Starting in late metaphase and through anaphase, the distribution of PAR-6 in P1 becomes skewed to the ventrolateral periphery, the part of the cell fated to give rise to EMS. PAR-6 is distributed uniformly at the AB periphery throughout the 2-cell stage. In the 4-cell stage, PAR-6 peripheral staining is strong in ABa, ABp and EMS, but PAR-6 can be detected only faintly around the periphery of P2 until metaphase of P2 at the 7-cell stage. At this time PAR-6 is asymmetrically localized to the dorsal side of P2, the part of the cell fated to give rise to C. The protein is distributed asymmetrically in P3 as well. Peripheral PAR-6 could be detected till about the 50-cell stage. |
|
|
|
Expr3682
|
|
WRM-1::GFP levels were high in the nucleus of the E blastomere at the eight-cell stage. However, a time course of images revealed that WRM-1::GFP is at first localized similarly in both newly formed nuclei at the beginning of telophase of the EMS cell division. Furthermore, even signal-nonresponsive cells, including cells present at the one-, two- and four-cell stages, exhibit nuclear accumulation of WRM-1 at the beginning of telophase. During the EMS cell division, the nuclear signal in MS grows weaker, while in E, the nuclear WRM-1::GFP levels become higher. A high WRM-1::GFP nuclear level during and after cytokinesis was only observed in signal-responding cells, including numerous posterior descendants of later a/p divisions. In addition to its change in nuclear levels, a cell cycle- and signal-dependent change in the localization of WRM-1 protein was also observed at the cell cortex and cell-cell contact sites. |
|
Previous data: analysis of the PAR proteins has focused primarily on their anterior-posterior localization at the 1-cell stage and their roles in subsequent anterior-posterior polarity. After cell division begins, however, this anterior-posterior asymmetry is reiterated only in the lineage of cells that form the germline. In contrast, some somatic (non-germline) cells show an apical-basal polarity in PAR localization. |
|
Expr1820
|
The apical-basal polarity of the PAR protein persists through early gastrulation, although the level of PAR-2 diminishes. Later changes in PAR distribution were not analyzed further. |
By the 4-cell stage, the posterior PAR protein PAR-2 is localized to basolateral surfaces, and is not detected on the apical surfaces of somatic cells. |
|
Previous data: analysis of the PAR proteins has focused primarily on their anterior-posterior localization at the 1-cell stage and their roles in subsequent anterior-posterior polarity. After cell division begins, however, this anterior-posterior asymmetry is reiterated only in the lineage of cells that form the germline. In contrast, some somatic (non-germline) cells show an apical-basal polarity in PAR localization. |
|
Expr1821
|
The apical-basal polarity of the PAR proteins persists through early gastrulation, cells in the interior of the embryo accumulate PAR-3 on their blastocoel-facing surfaces; these and later changes in PAR distribution were not analyzed further. |
By the middle of the 4-cell stage, the anterior PAR protein PAR-3 is present over the entire cortex of each somatic blastomere. However by the end of the 4-cell stage and at later stages PAR-3 is concentrated in a broad `cap' centered on the apical surface. |
|
Previous data: analysis of the PAR proteins has focused primarily on their anterior-posterior localization at the 1-cell stage and their roles in subsequent anterior-posterior polarity. After cell division begins, however, this anterior-posterior asymmetry is reiterated only in the lineage of cells that form the germline. In contrast, some somatic (non-germline) cells show an apical-basal polarity in PAR localization. |
|
Expr1822
|
The apical-basal polarity of the PAR proteins persists through early gastrulation, cells in the interior of the embryo accumulate PAR-6 on their blastocoel-facing surfaces; these and later changes in PAR distribution were not analyzed further. |
By the middle of the 4-cell stage, the anterior PAR protein PAR-6 is present over the entire cortex of each somatic blastomere. However by the end of the 4-cell stage and at later stages PAR-6 is concentrated in a broad `cap' centered on the apical surface. |
|
|
|
Expr16342
|
CDC-25.3::GFP signal detected at 4-cell stage in ABa/ABp. Using our AF correction method, we were able to observe clear nuclear localization already at the start of the four-cell stage and accurately track its accumulation and release at NEBD at a time at which AF almost completely masked its expression in uncorrected images. |
|
