Functional and hierarchical interactions among zebrafish <i>vox/vent</i> homeobox genes

Gilardelli, Claudio N.; Pozzoli, Ombretta; Sordino, Paolo; Matassi, Giorgio; Cotelli, Franco

doi:10.1002/dvdy.20073

Cited by 42 publications

(31 citation statements)

References 68 publications

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“…Alternatively, this result may reflect a temporal difference in Wnt8 and BMP regulation of vent/ vox/ved, consistent with our previous finding that Wnt8 fulfills an earlier requirement than BMP for limiting the organizer (Ramel and Lekven, 2004). Another possibility is that Vent, Vox, and Ved are different in their ability to repress organizer genes (Gilardelli et al, 2004).…”

Section: Wnt8 Bmp and Axial Versus Non-axial Mesoderm Specificationsupporting

confidence: 89%

“…In the pre-gastrula zebrafish, Wnt8 is the primary regulator of mesodermal vent, vox, and ved expression (Ramel and Lekven, 2004;Ramel et al, 2005). By 70% epiboly, mesodermal vent is primarily under BMP regulation, while mesodermal vox and ved expression continues to depend predominantly on Wnt8 (Kawahara et al, 2000a,b;Melby et al, 2000;Imai et al, 2001;Shimizu et al, 2002;Gilardelli et al, 2004;Ramel et al, 2005). In the absence of both Wnt8 and BMP signaling, all nascent mesoderm expresses an axial mesoderm fate.…”

Section: Wnt8 Bmp and Axial Versus Non-axial Mesoderm Specificationmentioning

confidence: 99%

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A direct role for Wnt8 in ventrolateral mesoderm patterning

Baker

Ramel

Lekven

2010

Developmental Dynamics

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Vertebrate dorsoventral patterning requires both Wnt8 and BMP signaling. Because of their multiple interactions, discerning roles attributable specifically to Wnt8 independent of BMP has been a challenge. For example, Wnt8 represses the dorsal organizer that negatively regulates ventral BMP signals, thus Wnt8 loss-of-function phenotypes may reflect the combined effects of reduced Wnt8 and BMP signaling. We have taken a loss-of-function approach in the zebrafish to generate embryos lacking expression of both Wnt8 and the BMP antagonist Chordin. wnt8;chordin loss-of-function embryos show rescued BMP signaling, thereby allowing us to identify Wnt8-specific requirements. Our analysis shows that Wnt8 is uniquely required to repress prechordal plate specification but not notochord, and that Wnt8 signaling is not essential for specification of tailbud progenitors but is required for normal expansion of posterior mesoderm cell populations. Thus, Wnt8 and BMP signaling have independent roles during vertebrate ventrolateral mesoderm development that can be identified through loss-of-function analysis. Developmental Dynamics 239:2828-2836,

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Section: Wnt8 Bmp and Axial Versus Non-axial Mesoderm Specificationsupporting

confidence: 89%

Section: Wnt8 Bmp and Axial Versus Non-axial Mesoderm Specificationmentioning

confidence: 99%

A direct role for Wnt8 in ventrolateral mesoderm patterning

Baker

Ramel

Lekven

2010

Developmental Dynamics

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“…a-Elongation Factor 1a (EF1a) was used as positive control, using specific primers as described (Gilardelli et al, 2004).…”

Section: Multi-tissue Rt-pcrmentioning

confidence: 99%

Characterization of the AP‐1 μ1A and μ1B adaptins in zebrafish (Danio rerio)

Zizioli

Forlanelli

Guarienti

et al. 2010

Developmental Dynamics

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Protein transport between the trans-Golgi network and endosomes is mediated by transport vesicles formed by the adaptor-protein complex AP-1, consisting of the adaptins g1, b1, m1, s1. Mammalia express m1A ubiquitously and isoform m1B in polarized epithelia. Mouse g1 or m1A 'knock out's revealed that AP-1 is indispensable for embryonic development. We isolated m1A and m1B from Danio rerio. Analysis of m1A and m1B expression revealed tissue-specific expression for either one during embryogenesis and in adult tissues in contrast to their expression in mammalia. m1B transcript was detected in organs of endodermal derivation and ''knock-down'' experiments gave rise to embryos defective in formation of intestine, liver, and pronephric ducts. Development ceased at 7-8 dpf. m1B is not expressed in murine liver, indicating loss of m1B expression and establishment of alternative sorting mechanisms during mammalian development. Developmental Dynamics 239:2404-2412,

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“…Among them, Id-1 encodes a protein that acts as a positive regulator of cell proliferation and a negative regulator of cell differentiation (24). Xvent1 is another BMP direct target gene, which is a member of the vox/vent homeobox gene family and is involved in dorsoventral axis determination (25). We studied the effect of PPM1A on the transcriptional activity of these target genes.…”

Section: Ppm1amentioning

confidence: 99%

Protein Serine/Threonine Phosphatase PPM1A Dephosphorylates Smad1 in the Bone Morphogenetic Protein Signaling Pathway

Duan

Liang

Feng

et al. 2006

Journal of Biological Chemistry

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Bone morphogenetic proteins (BMPs) are secreted polypeptides belonging to the transforming growth factor-␤ (TGF-␤) superfamily that activates a broad range of biological responses in the metazoan organism. The BMP-initiated signaling pathway is under tight control by processes including regulation of the ligands, the receptors, and the key downstream intracellular effector Smads. A critical point of control in BMP signaling is the phosphorylation of Smad1, Smad5, and Smad8 in their C-terminal SXS motif. Although such phosphorylation, which is mediated by the type I BMP receptor kinases in response to BMP stimulation, is well characterized, biochemical mechanisms underlying Smad dephosphorylation remain to be elucidated. In this study, we have found that PPM1A, a metal ion-dependent protein serine/threonine phosphatase, physically interacts with and dephosphorylates Smad1 both in vitro and in vivo. Functionally, overexpression of PPM1A abolishes BMP-induced transcriptional responses, whereas RNA interference-mediated knockdown of PPM1A enhances BMP signaling. Collectively, our study suggests that PPM1A plays an important role in controlling BMP signaling through catalyzing Smad dephosphorylation.Bone morphogenetic proteins (BMPs), 3 originally identified by their ability to cause bone differentiation (1), are signaling molecules that belong to the transforming growth factor-␤ (TGF-␤) superfamily. Presently, the biological functions of BMPs have been greatly expanded. BMPs regulate skeletal development as well as many non-osteogenic developmental processes, such as mesoderm patterning, left-right symmetry, neuronal patterning, and hematopoiesis (2-5). Accumulating evidence indicates that BMPs play an important role in the regulation of stem cell properties (3, 6 -8). Signals from BMP ligands are transduced through binding to type I and II receptors on the cell surface, where type II receptors activate type I receptors, which in turn phosphorylate the downstream Smad1, Smad5, and Smad8. The phospho-R-Smads (P-Smads) form a complex with Smad4 and translocate into the nucleus, where they bind to the Smad binding sites and cooperate with other transcription factors to regulate BMP-induced gene expression (5, 9, 10).Despite substantial effort devoted to understanding the actions of BMP/TGF-␤ and Smads, the precise regulation of Smads remains enigmatic. Regulation of Smads can be accomplished via various post-translational mechanisms, including phosphorylation and ubiquitin-dependent modifications (11,12). Among these, BMP-induced phosphorylation of Smad1/ 5/8, which is carried out by the BMP type I receptor (BMPRIA or BMPRIB) and occurs at the C-terminal SXS motif of Smad1/ 5/8, represents the most critical step in Smad signaling. The SXS phosphorylation triggers a cascade of intracellular events from Smad complex assembly in the cytoplasm to transcriptional control in the nucleus.The reversible phosphorylation and dephosphorylation represents a fundamental strategy used by eukaryotic organisms to regulate a battery of...

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Functional and hierarchical interactions among zebrafish vox/vent homeobox genes

Cited by 42 publications

References 68 publications

A direct role for Wnt8 in ventrolateral mesoderm patterning

A direct role for Wnt8 in ventrolateral mesoderm patterning

Characterization of the AP‐1 μ1A and μ1B adaptins in zebrafish (Danio rerio)

Protein Serine/Threonine Phosphatase PPM1A Dephosphorylates Smad1 in the Bone Morphogenetic Protein Signaling Pathway

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