Néant I , Leung HC , Webb SE , Miller AL , Moreau M , Leclerc C .

ITCPD/17-9 Innovation and Technology Commission - Hong Kong (Innovation and Technology Commission of Hong Kong Special Administrative Government)

	Figiure 1. Expression of CaV1.2 mRNA in X. laevis. (A) RT-qPCR analysis of Cav1.1, Cav1.2, Cav1.3 and Cav1.4 in ectoderm (animal caps) isolated before gastrulation at stages 8 and 9. The expression levels were normalized to the housing keeping gene odc (ornithine decarboxylase). The level Cav1.2 mRNA was significantly higher than that of Cav1.1, Cav1.3 and Cav1.4 (one way ANOVA with Bonferroni’s test, ****P < 0.0001). The data represent mean ± SEM of 9 independent experiments such that 20 animal caps were used for each experiment. (B) In situ hybridization to show the pattern of localization of CaV1.2 mRNA in sections acquired at early gastrula (stage 10). (Ba) Photomicrograph of a sagittal section labelled with the anti-sense probe, which shows CaV1.2 expression in the ectoderm (ect) and dorsal mesoderm (mes). There is no CaV1.2 expression in the ventral mesoderm. (Bb) Higher magnification view of the ectoderm (corresponding to the white dashed rectangle in panel (Ba), which shows that CaV1.2 is expressed in the internal layer (int) but not in the external layer (ext). (Bc) Photomicrograph of a sagittal section showing no labelling with the sense probe. In (Ba-Bc), dorsal is to the right and the arrows indicate the dorsal blastopore groove. Scale bars are 300 µm.
	Figure 2. trpc1 is expressed in the ectoderm of blastula and gastrula stage embryos. Spatial expression of trpc1 mRNA in blastula and gastrula stage embryos. Whole mount in situ hybridization was performed on embryos fixed at blastula (stage 9), early gastrula (stage 10.5) and late gastrula (stage 11.5). (A) Expression of trpc1 at stage 9 in an intact embryo (animal pole view), showing that the ectoderm is labelled. (B) Sagittal section taken through the embryo shown in panel A, indicating trpc1 expression in the ectoderm alone; the mesoderm and endoderm were not labelled. (C) Expression of trpc1 in an intact embryo at stage 10.5 (animal pole view). (D) Sagittal section taken through the embryo shown in panel (C), showing trpc1 expression in the ectoderm, with no difference in the level of expression between the dorsal and the ventral sides. (E) Expression of trpc1 in an intact embryo at stage 11.5 (animal pole view). (F) Sagittal section taken through the embryo shown in panel E. AP, VP, ect, mes, end and Bl are animal pole, vegetal pole, ectoderm, mesoderm endoderm and blastocoel, respectively. In panels (D) and (F), dorsal is to the right and the arrows indicate the blastopore lip. Scale bar is 300 µm.
	Figure 3. Pattern of localization of Trpc1 in gastrula stage embryos. (A) Single optical view of a sagittal section taken though a gastrula stage embryo, showing the localization of Trpc1 in the ectoderm (ect) and mesoderm (mes). There is a lower level of Trpc1 expression in the endoderm (end). The arrow indicates the position of the blastopore lip. The regions bounded by the dashed white rectangles are shown at higher magnification in panels (B–D). These images show that at the cellular level, Trpc1 is localized mainly in the plasma membrane. Trpc1 localization, shown in green, was revealed with the rabbit anti-Trpc1 polyclonal antibody and an Alexa-555-conjugated anti-rabbit secondary antibody. The nuclei (in blue) were labelled with ToPro3. Scale bars are 300 µm in panel (A), and 40 µm in panels (B–D).
	Figure 4. Trpc1 knock down reduces the expression of Trpc1 in the ectoderm and abolishes the increase in intracellular Ca2+ generated following activation of CaV1.2 channels in animal cap explants. (A–D) Embryos at the 2-cell stage were injected with (A–C) control-MO or (B–D) TRPC1-MO1 into both blastomeres, and the expression of Trpc1 was revealed by immunostaining at the blastula stage. (A,B) Confocal view of sagittal section taken through the entire embryo. (C,D) Confocal view at the level of the ectoderm. trpc1 knock-down impaired the expression of Trpc1. The nuclei (in blue) were labelled with ToPro3. Scale bars are 350 µm in (A,B) and 40 µm in (C,D). (E,F) Relative changes in fluorescence (F/F0) revealing changes in intracellular Ca2+ generated in single animal caps loaded with the Ca2+-indicator Fluo4 and isolated from embryos injected with either (E) control-MO or (F) TRPC1-MO1. The data are plotted as the mean of F/F0 (red traces) + SEM (black bars) from 7 (E) or 10 (F) randomly selected fields within a single animal cap. Noggin (2 µg/mL) was added (blue arrows) within the first 10 min after the start of data acquisition. Additional data are provided in Figure S3.
	Figure 5. Membrane depolarisation induced by noggin in the ectoderm requires Trpc1. Control morpholino (CMO) or TRPC1-MO1 was injected into both blastomeres of 2-cell stage embryos. Animal caps were then prepared at late blastula (stage 9) and loaded with the potentiometric dye DiBAC4(3). (A,B) The mean calculated membrane potential revealed membrane depolarisation following the addition of noggin (3 µg/mL, see blue arrow) in animal caps prepared from (A) CMO- or (B) TRPC1-MO1-injected embryos (n = 4 for each). (C,D) The mean calculated membrane potential in isolated ectoderm cells (n = 5 cells) that were dissociated from animal caps prepared from (C) CMO- or (D) TRPC1-MO1-injected embryos. (E) A box plot showing the maximal depolarisation values reached after noggin stimulation of animal caps or dissociated ectoderm cells prepared from CMO-injected embryos (white bars) or TRPC1-MO1-injected embryos (grey bars). The maximal depolarisation values for the animal caps and dissociated cells prepared from CMO- and TRPC1-MO1 embryos were significantly different, (Mann-Whitney test with *P < 0.02 for animal cap recordings, and **P < 0.004 for dissociated cell recordings).
	Figure 6. trpc1 knock-down impairs the expression of the early neural gene, zic3. Embryos were co-injected at the 8-cell stage into a single dorsal animal blastomere with nuclear β-galactosidase mRNA and: (A) the standard control-MO, (B) a splice-blocking MO (TRPC1 -MO3), (C) TRPC1- MO1, or (D) TRPC1- MO1 plus r-trpc1 mRNA. Embryos were then fixed at stage 14 for subsequent whole-mount in situ hybridization of zic3; see red arrowheads in panel (A). The side of the embryo injected with MO ± r-trpc1-mRNA was confirmed by reaction of β-galactosidase with X-Gal, as shown by the blue labelling on the right side of each embryo; see white arrowhead in panel (A). Scale bar is 500 µm. (E) A bar chart showing the mean ± S.E.M. (n = 17) ratio of the area of zic3 expression on the injected and un-injected sides of the embryo. The asterisks indicate data that are significantly different at p < 0.001 when using one-way ANOVA and the Tukey’s honest significance post-hoc test.
	Figure 7. The tail domain of BMPRII is essential for the interaction with Trpc1, and noggin modulates the BMPRII-Trpc1 interaction. (A) Schematic illustration of the full-length BMPRII and the tail domain-deleted construct (BRII-∆TD). The yellow, black, grey and red rectangles show the signal peptide (SP); transmembrane domain (TM), kinase domain, and tail domain respectively. (B) Representative western blots showing the immunoprecipitation data acquired when analysing the protein-protein interaction between BMPRII and Trpc1. Embryos at the 4-cell stage were either injected (+) or not (−) with BMPRII-HA (200 pg/cell) or BRII-∆TD-HA (200 pg/cell), along with Myc-Trpc1 (200 pg/cell) into all the blastomeres. Animal caps were then prepared at stage 8–9, lysed and subjected to immunoprecipitation. ns, non-specific band. Western blot data were revealed by enhanced chemiluminescence (ECL; n = 4 independent experiments). (C) Representative western blots showing the interaction between BMPRII and TRPC1 in the presence of noggin. Animal caps were collected at stage 8–9 from embryos injected with BMPRII-HA (200 pg/cell) and Myc-Trpc1 (200 pg/cell) into all the blastomeres at the 4-cell stage, after which they were either incubated (+) or not (−) with 2 µg/mL noggin for 15 min, and then lysed and subjected to immunoprecipitation with anti-Myc antibody. The western blot data were revealed by ECL (n = 3 independent experiments). (D) Quantification of the BMPRII-HA fraction associated with Myc-Trpc1. Ratios of co-immunoprecipitated BMPRII-HA: Myc-Trpc1 were calculated in the absence or presence of noggin using the Bio-Rad ChemiDoc Image Lab software 5.2.1. There data represent the mean ± from 3 independent experiments. The asterisk indicates data that are significantly different at p < 0.05 when using the Mann-Whitney test. The full-length blots are presented in Supplementary figure S7.
	Figure 8. Hypothetical model to depict the role of Trpc1 channels in linking the inhibition of BMP pathway by noggin, and the activation of Cav1.2 channels in ectodermal cells. During gastrulation, the cells of the embryonic ectoderm have the choice between two fates; they can give rise to either epidermal or neural progenitors. In the plasma membrane, the molecular components involved in this choice are BMP receptors type I (BmprI) and type II (BmprII), Trpc1 and voltage-dependent Ca2+ channels (Cav1.2). The membrane potential in the ectoderm is ~−60 mV; i.e., the interior is negatively charged62. (A) Induction of the epidermis occurs through a signalling cascade, which involves the binding of Bmp4 to its receptor, and then the transphosphorylation of BmprII by BmprI. This is followed by the activation of Smads, which translocate into the nucleus to form active transcriptional complexes to control the expression of epidermal genes. In this scenario, there is no interaction between Trpc1 and BmprII, and Cav1.2 remains inactive. (B) During neural induction, noggin binds to BMP4, and thus prevents the activation of the BMP pathway. As a consequence, it induces a physical interaction between BmprII and Trpc1 channels. This interaction leads to the activation of Trpc1, which either alone or associated with other Trp channels (e.g., Trpv4), triggers an influx of cations (Ca2+ and Na+). This influx of cations depolarizes the membrane (i.e., there is more positive charge inside) up to a threshold sufficient to open the voltage-gated Ca2+ channel, Cav1.2. As we have previously shown27,29, the resulting influx of Ca2+ is then sufficient to activate the expression.
	Figure S1: Expression of CaV1.x mRNA in X. laevis. (A) RT-qPCR analysis of Cav1.1, Cav1.2, Cav1.3 and Cav1.4 in ectoderm (animal caps) isolated at mid-gastrula (stage 10.5). The expression levels were normalized to the housing keeping gene odc (ornithine decarboxylase). The expression level Cav1.2 mRNA was significantly higher than that of Cav1.1, Cav1.3 and Cav1.4, in animal caps (one way ANOVA with Bonferroni’s test, ****P<0.0001). The data represent the mean ± SEM of 4 independent experiments, with 20 animal caps being used for each experiment. (B) RT-qPCR analysis of Cav1.2 in ectoderm (animal caps) isolated from embryos before gastrulation (stage 8 and stage 9) and at midgastrula (stage 10.5). The expression levels were normalized to the housing keeping gene odc (ornithine decarboxylase). No significant changes in Cav1.2 mRNA levels occurred during these 3 stages (one-way ANOVA with Bonferroni’s test, P<0.05). The data represent the mean ± SEM of 4 and 5 independent experiments for stage 8 and 10.5, and for stage 9, respectively, such that in each experiment there were 20 animal caps. (C-D) Histograms to show RT-qPCR analysis of Cav1.2 (C) and of Cav1.1, Cav1.3 and Cav1.4 (D) in control stage 9 animal caps and in noggin-treated stage 9 animal caps. The level of expression was normalized to the housing keeping gene odc (ornithine decarboxylase). No significant changes in the mRNA levels of Cav1.1, Cav1.2, Cav1.3, and Cav1.4 were observed when comparing control and noggin-treated animal caps (Mann-Whitney test). The data represent the mean ± SEM of 10 independent experiments, with 20 animal caps per experiment.
	Figure S2: Expression of trpc1, trpp2, trpv4 and orai1 mRNA in X. laevis. (A) RT-qPCR analysis of trpc1 in ectoderm (animal caps) isolated from embryos before gastrulation (stage 8 and stage 9) and at mid-gastrula (stage 10.5). In each case, the level of expression was normalized to the housing keeping gene odc (ornithine decarboxylase). No significant changes in mRNA levels occurred during these 3 developmental stages (one-way ANOVA with Bonferroni’s test, P<0.05). The data represent the mean ± SEM of 7 independent experiments for each of the 3 stages, and 20 animal caps were collected for each experiment. (B) RT-qPCR analysis of trpc1 in control stage 9 animal caps and in noggin-treated stage 9 animal caps. In each case, the level of expression was normalized to the housing keeping gene odc (ornithine decarboxylase). When compared with the control animal caps, no significant changes in trpc1 mRNA levels occurred in the noggin-treated animal caps (MannWhitney t-test). The data represent the mean ± SEM of 9 independent experiments, with 20 animal caps in each experiment. (C) RT-qPCR analysis of trpp2, trpv4 and orai1 in ectoderm (animal caps) isolated from embryos before gastrulation (stage 8 and stage 9) and at mid-gastrula (stage 10.5). In each case, the level of expression was normalized to the housing keeping gene odc (ornithine decarboxylase). The data represent the mean ± SEM of 5 independent experiments for each of the 3 stages with 20 animal caps per experiment. (D) Early embryos and animal caps express the long trpc1 isoform. EcoRV treatment of trpc1-PCR products systematically cleaved the 117-bp amplicon into 2 fragments of 63 bp and 54 bp as shown on the polyacrylamide gel. This was shown in maternal stage (Stage 2; St2) embryos as well as in animal caps at blastula (St 8 and St9) and gastrula (St 10.5). The sequence shows that the amplicon exhibits a conserved EcoRV site (in red), in the 21bp-longer isoform (bold in box). The full-length gels are presented in supplementary figure S8.
	Figure S3: Trpc1 knock down abolishes the increase in intracellular Ca2+ generated following the activation of CaV1.2 channels in animal cap explants. (A-B) Relative changes in fluorescence (F/F0) reveal changes in intracellular Ca2+ generated in a single animal cap loaded with the Ca2+ -indicator Fluo4 after being isolated from an embryo injected with either (A) control-MO or (B) TRPC1-MO1. In (A) panels (a-d), and in (B) panels (a-c), the graphs show examples of 4 and 3 independent experiments, respectively. Values are plotted as the F/F0 mean (red traces) + SEM (black bars) from 4 (A) or 10 (B) randomly selected fields within a single animal cap. Noggin (3 µg/mL) was added (blue arrows) within the first 10 min after the start of data acquisition.
	Figure S4: trpc1 knock-down impairs the expression of the early neural gene, sox2. Embryos were co-injected at the 8-cell stage into a single dorsal animal blastomere with nuclear β-galactosidase mRNA (150 pg) and either (A,B) the standard control-MO (CMO; 17 ng) or (C-F) TRPC1-MO1 (17 ng). Embryos were then fixed at stage 14 for subsequent whole-mount in situ hybridization for sox2; see black arrows. The side of the embryo injected with MO was confirmed by reaction of β-galactosidase with Red-Gal, as shown by the red labelling on each embryo; see red arrows. (A-B) Images from 2 different embryos injected with CMO showing similar levels of sox2 expression on the left and right side of the embryos. (C-F) Images from 4 different embryos injected with TRPC1-MO1 showing that the expression of sox2 was reduced (see black arrows) on the injected side. Scale bar 500 µm
	Figure S5: Trpc1 channels are co-expressed with BMPRII. Immunostaining of Trpc1 protein in anterior ectoderm of a representative stage 10 embryo. Xenopus BMPRII-HA (200 pg/cell) was injected into all the blastomeres of 4-cell embryos. The presence of HA-tagged BMPRII proteins and Trpc1 were revealed with an anti-HA antibody and a rabbit anti-Trpc1 polyclonal primary antibody, respectively. The secondary antibodies were Alexa-555-conjugated anti-mouse and Alexa-488- conjugated anti-rabbit for HA-tagged BMPRII and Trpc1, respectively. These images show the same confocal plane and indicate the co-expression of BMPRII-HA with Trpc1, which appears in yellow (see white arrows). Scale bar represents 30 µm.
	Figure S6. The truncated form of BmprRII (BmprII-deltaTD) has no neural inducing activity. RT-qPCR analysis of two neural genes, zic3 (A) and sox2 (B), and two genes controlling epidermal fate, msx1 (C) and bmp4 (D), in noggin-treated stage 9 animal caps (grey bars), in animal caps over-expressing bmprII-deltaTD (black bars) and in control animal caps (white bars). Expression was normalized to the housing keeping gene odc (ornithine decarboxylase). When comparing the level of expression of these 4 genes in animal caps over-expressing bmprII-deltaTD, with the level of expression in noggin treated and control animal caps, these data indicate that bmprII-deltaTD has no neural inducing activity, (one way ANOVA with Bonferroni’s test, **P<0.001, ****P<0.0001). The data represent the mean ± SEM of 8 independent experiments, with 20 animal caps in each experiment.
	Supplementary figure S7. Full blot images of results shown in figure 7.
	Supplementary figure S8. Full images of undigested and EcoRV-digested trpc1-amplicons on polyacrylamide gels shown in Figure S2D.
	cacna1c (calcium channel, voltage-dependent, L type, alpha 1C subunit ) gene expression in bisected Xenopus laevis embryo, assayed via in situ hybridization. NF stage 10 (a) and in higher magnification (b) . Key ect= ectoderm, mes= dorsal [endo]mesoderm and ext/int = outer versus inner layer of animal cap ectoderm.
	Figure 1. Expression of CaV1.2 mRNA in X. laevis. (A) RT-qPCR analysis of Cav1.1, Cav1.2, Cav1.3 and Cav1.4 in ectoderm (animal caps) isolated before gastrulation at stages 8 and 9. The expression levels were normalized to the housing keeping gene odc (ornithine decarboxylase). The level Cav1.2 mRNA was significantly higher than that of Cav1.1, Cav1.3 and Cav1.4 (one way ANOVA with Bonferroni’s test, ****P < 0.0001). The data represent mean ± SEM of 9 independent experiments such that 20 animal caps were used for each experiment. (B) In situ hybridization to show the pattern of localization of CaV1.2 mRNA in sections acquired at early gastrula (stage 10). (Ba) Photomicrograph of a sagittal section labelled with the anti-sense probe, which shows CaV1.2 expression in the ectoderm (ect) and dorsal mesoderm (mes). There is no CaV1.2 expression in the ventral mesoderm. (Bb) Higher magnification view of the ectoderm (corresponding to the white dashed rectangle in panel (Ba), which shows that CaV1.2 is expressed in the internal layer (int) but not in the external layer (ext). (Bc) Photomicrograph of a sagittal section showing no labelling with the sense probe. In (Ba-Bc), dorsal is to the right and the arrows indicate the dorsal blastopore groove. Scale bars are 300 µm.

Ambudkar, TRPC1, Orai1, and STIM1 in SOCE: Friends in tight spaces. 2017, Pubmed

Ambudkar, TRPC1, Orai1, and STIM1 in SOCE: Friends in tight spaces. 2017, Pubmed
Aramaki, Jiraiya attenuates BMP signaling by interfering with type II BMP receptors in neuroectodermal patterning. 2010, Pubmed , Xenbase
Ashworth, Buffering intracellular calcium disrupts motoneuron development in intact zebrafish embryos. 2001, Pubmed
Batut, The Ca2+-induced methyltransferase xPRMT1b controls neural fate in amphibian embryo. 2005, Pubmed , Xenbase
Bobanovic, Molecular cloning and immunolocalization of a novel vertebrate trp homologue from Xenopus. 1999, Pubmed , Xenbase
Catterall, International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels. 2005, Pubmed
Chalmers, Intrinsic differences between the superficial and deep layers of the Xenopus ectoderm control primary neuronal differentiation. 2002, Pubmed , Xenbase
Clapham, TRP channels as cellular sensors. 2003, Pubmed
Créton, Patterns of free calcium in zebrafish embryos. 1998, Pubmed
De Robertis, Dorsal-ventral patterning and neural induction in Xenopus embryos. 2004, Pubmed , Xenbase
Dietrich, Classical Transient Receptor Potential 1 (TRPC1): Channel or Channel Regulator? 2014, Pubmed
Drean, Expression of L-type Ca2+ channel during early embryogenesis in Xenopus laevis. 1995, Pubmed , Xenbase
Epps, Characterization of the steady-state and dynamic fluorescence properties of the potential-sensitive dye bis-(1,3-dibutylbarbituric acid)trimethine oxonol (Dibac4(3)) in model systems and cells. 1994, Pubmed
Frisch, XBMPRII, a novel Xenopus type II receptor mediating BMP signaling in embryonic tissues. 1998, Pubmed , Xenbase
Futel, TRPP2-dependent Ca2+ signaling in dorso-lateral mesoderm is required for kidney field establishment in Xenopus. 2015, Pubmed , Xenbase
Hackley, A transiently expressed connexin is essential for anterior neural plate development in Ciona intestinalis. 2013, Pubmed
Hassel, Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry. 2004, Pubmed
Helton, Neuronal L-type calcium channels open quickly and are inhibited slowly. 2005, Pubmed
Hemmati-Brivanlou, Vertebrate neural induction. 1997, Pubmed , Xenbase
Ichikawa, TRPC6 regulates cell cycle progression by modulating membrane potential in bone marrow stromal cells. 2014, Pubmed
Kishi, Requirement of Sox2-mediated signaling for differentiation of early Xenopus neuroectoderm. 2000, Pubmed , Xenbase
Kobori, The transient receptor potential channels TRPP2 and TRPC1 form a heterotetramer with a 2:2 stoichiometry and an alternating subunit arrangement. 2009, Pubmed
Kuroda, Default neural induction: neuralization of dissociated Xenopus cells is mediated by Ras/MAPK activation. 2005, Pubmed , Xenbase
Kuroda, Neural induction in Xenopus: requirement for ectodermal and endomesodermal signals via Chordin, Noggin, beta-Catenin, and Cerberus. 2004, Pubmed , Xenbase
Lamb, Neural induction by the secreted polypeptide noggin. 1993, Pubmed , Xenbase
Leclerc, L-type calcium channel activation controls the in vivo transduction of the neuralizing signal in the amphibian embryos. 1997, Pubmed
Leclerc, Calcium transients triggered by planar signals induce the expression of ZIC3 gene during neural induction in Xenopus. 2003, Pubmed , Xenbase
Leclerc, Role of dihydropyridine-sensitive calcium channels in meiosis and fertilization in the bivalve molluscs Ruditapes philippinarum and Crassostrea gigas. 2000, Pubmed
Leclerc, Imaging patterns of calcium transients during neural induction in Xenopus laevis embryos. 2000, Pubmed , Xenbase
Leclerc, The calcium: an early signal that initiates the formation of the nervous system during embryogenesis. 2012, Pubmed
Leclerc, Calcium transients and calcium signalling during early neurogenesis in the amphibian embryo Xenopus laevis. 2006, Pubmed , Xenbase
Lee, FGF-activated calcium channels control neural gene expression in Xenopus. 2009, Pubmed , Xenbase
Ma, Heteromeric TRPV4-C1 channels contribute to store-operated Ca(2+) entry in vascular endothelial cells. 2011, Pubmed
Ma, Identification of neurogenin, a vertebrate neuronal determination gene. 1996, Pubmed , Xenbase
Miyazono, Bone morphogenetic protein receptors and signal transduction. 2010, Pubmed
Mizuseki, Xenopus Zic-related-1 and Sox-2, two factors induced by chordin, have distinct activities in the initiation of neural induction. 1998, Pubmed , Xenbase
Moreau, Increased internal Ca2+ mediates neural induction in the amphibian embryo. 1994, Pubmed
Moreau, Ca(2+) coding and decoding strategies for the specification of neural and renal precursor cells during development. 2016, Pubmed
Nakata, Xenopus Zic3, a primary regulator both in neural and neural crest development. 1997, Pubmed , Xenbase
Neant, The RNA-binding protein Xp54nrb isolated from a Ca²+-dependent screen is expressed in neural structures during Xenopus laevis development. 2011, Pubmed , Xenbase
Néant, Kcnip1 a Ca²⁺-dependent transcriptional repressor regulates the size of the neural plate in Xenopus. 2015, Pubmed , Xenbase
Ong, A TRPC1 protein-dependent pathway regulates osteoclast formation and function. 2013, Pubmed
Palmer, Some bio-electric parameters of early Xenopus embryos. 1970, Pubmed , Xenbase
Papanayotou, Calfacilitin is a calcium channel modulator essential for initiation of neural plate development. 2013, Pubmed
Peng, Xenopus laevis: Practical uses in cell and molecular biology. Solutions and protocols. 1991, Pubmed , Xenbase
Plásek, Slow fluorescent indicators of membrane potential: a survey of different approaches to probe response analysis. 1996, Pubmed
Reuter, Calcium channel modulation by neurotransmitters, enzymes and drugs. , Pubmed
Roth, A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription. 1991, Pubmed , Xenbase
Satow, Dullard promotes degradation and dephosphorylation of BMP receptors and is required for neural induction. 2006, Pubmed , Xenbase
Shim, XTRPC1-dependent chemotropic guidance of neuronal growth cones. 2005, Pubmed , Xenbase
Stern, Neural induction: old problem, new findings, yet more questions. 2005, Pubmed , Xenbase
Suzuki, Xenopus msx1 mediates epidermal induction and neural inhibition by BMP4. 1997, Pubmed , Xenbase
Venkatachalam, TRP channels. 2007, Pubmed
Waggoner, Dye indicators of membrane potential. 1979, Pubmed
Wang, Hypoxia inducible factor-1-dependent up-regulation of BMP4 mediates hypoxia-induced increase of TRPC expression in PASMCs. 2015, Pubmed
Webb, Ca2+ signalling and early embryonic patterning during zebrafish development. 2007, Pubmed
Wen, BMP gradients steer nerve growth cones by a balancing act of LIM kinase and Slingshot phosphatase on ADF/cofilin. 2007, Pubmed , Xenbase
Wilson, Induction of epidermis and inhibition of neural fate by Bmp-4. 1995, Pubmed , Xenbase
Wölfle, Involvement of nonselective cation channels in the depolarisation initiating vasomotion. 2010, Pubmed
Zimmerman, The Spemann organizer signal noggin binds and inactivates bone morphogenetic protein 4. 1996, Pubmed , Xenbase