Human Crossveinless-2 is a novel inhibitor of bone morphogenetic proteins

Binnerts, M.E.; Wen, Xiaohui; Canté-Barrett, Kirsten; Bright, Jessica M.; Chen, Huang-Tsu; Asundi, Vinod K.; Sattari, Peter; Tang, Tom; Boyle, Bryan; Funk, Walter D.; Rupp, Fabio

doi:10.1016/j.bbrc.2004.01.048

Cited by 68 publications

(75 citation statements)

References 34 publications

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“…Previous studies showed that CV2 could be a pro-or anti-BMP factor, depending on different contexts (24 -26, 43, 44). In vitro, CV2 at excessive doses inhibited the BMP-dependent differentiation of osteoblast and chondrocyte in cell culture (25). The transfection of 293T cells with a CV2 cDNA-containing plasmid reduced cellular response to BMP-4 in a BMP-responding luciferase reporter assay (43).…”

Section: Discussionmentioning

confidence: 99%

“…Binding-It has been shown that CHL2, CV2, chordin, and Tsg inhibited BMP activity in a competitive manner in vitro (21,25,33,36). Co-precipitation experiment showed that CHL2 and chordin competed with type I receptors (BMPR-IA or BMPR- , 1000 nM chordin-VWC1 (f), 3000 nM CHL2-VWC3 (g), 4000 nM chordin-VWC3 (h), and 4000 nM CHL2-VWC1 (i), respectively, and 50 nM BMP-2 alone (j), were injected over the chip surface.…”

Section: Competition Of Modulator Proteins With Receptors For Bmp-2mentioning

confidence: 99%

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von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

Zhang

Huang

Qiu

et al. 2007

Journal of Biological Chemistry

130

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Section: Discussionmentioning

confidence: 99%

Section: Competition Of Modulator Proteins With Receptors For Bmp-2mentioning

confidence: 99%

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

Zhang

Huang

Qiu

et al. 2007

Journal of Biological Chemistry

130

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“…We identified the secreted BMP-binding protein Cvl2 as playing a crucial role in locally enhancing BMP activity in the two distinct domains at the NPB. Cvl2 has been described as both an activator and inhibitor of BMP signalling (Conley et al, 2000;Moser et al, 2003;Binnerts et al, 2004;Kamimura et al, 2004;Ambrosio et al, 2008). Like many other proteins that interact with BMPs, such as the BMP antagonist Chordin, Cvl2 contains cysteine-rich domains (Conley et al, 2000).…”

Section: Cvl2 Locally Enhances Bmp Activity At the Npb And Is Requirementioning

confidence: 99%

A BMP regulatory network controls ectodermal cell fate decisions at the neural plate border

2013

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SUMMARYDuring ectodermal patterning the neural crest and preplacodal ectoderm are specified in adjacent domains at the neural plate border. BMP signalling is required for specification of both tissues, but how it is spatially and temporally regulated to achieve this is not understood. Here, using a transgenic zebrafish BMP reporter line in conjunction with double-fluorescent in situ hybridisation, we show that, at the beginning of neurulation, the ventral-to-dorsal gradient of BMP activity evolves into two distinct domains at the neural plate border: one coinciding with the neural crest and the other abutting the epidermis. In between is a region devoid of BMP activity, which is specified as the preplacodal ectoderm. We identify the ligands required for these domains of BMP activity. We show that the BMP-interacting protein Crossveinless 2 is expressed in the BMP activity domains and is under the control of BMP signalling. We establish that Crossveinless 2 functions at this time in a positive-feedback loop to locally enhance BMP activity, and show that it is required for neural crest fate. We further demonstrate that the Distal-less transcription factors Dlx3b and Dlx4b, which are expressed in the preplacodal ectoderm, are required for the expression of a cell-autonomous BMP inhibitor, Bambi-b, which can explain the specific absence of BMP activity in the preplacodal ectoderm. Taken together, our data define a BMP regulatory network that controls cell fate decisions at the neural plate border.

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“…Drosophila, zebrafish and mammalian Cv2 proteins can also inhibit signaling in some, but not all, in vitro assays (e.g. Binnerts et al, 2004;Esterberg and Fritz, 2009;Harada et al, 2008;Kelley et al, 2009;Moser et al, 2003;Serpe et al, 2008;.…”

Section: Context-dependent Effects On Bmp Signal Reception: Crossveinmentioning

confidence: 99%

The extracellular regulation of bone morphogenetic protein signaling

2009

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In many cases, the level, positioning and timing of signaling through the bone morphogenetic protein (BMP) pathway are regulated by molecules that bind BMP ligands in the extracellular space. Whereas many BMP-binding proteins inhibit signaling by sequestering BMPs from their receptors, other BMP-binding proteins cause remarkably context-specific gains or losses in signaling. Here, we review recent findings and hypotheses on the complex mechanisms that lead to these effects, with data from developing systems, biochemical analyses and mathematical modeling.

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Human Crossveinless-2 is a novel inhibitor of bone morphogenetic proteins

Cited by 68 publications

References 34 publications

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

von Willebrand Factor Type C Domain-containing Proteins Regulate Bone Morphogenetic Protein Signaling through Different Recognition Mechanisms

A BMP regulatory network controls ectodermal cell fate decisions at the neural plate border

The extracellular regulation of bone morphogenetic protein signaling

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