The genetic basis of mammalian neurulation

Copp, Andrew J.; Greene, Nicholas D. E.; Murdoch, J.

doi:10.1038/nrg1181

Cited by 617 publications

(588 citation statements)

References 101 publications

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“…Interestingly, Lrp5͞6 are most closely associated with canonical Wnt pathways, although attention has recently been drawn to PCP mechanisms in neurulation (34). Three mutations of Lrp6-null (7), hypomorphic (9), and hypermorphic (present report) are now associated with NTD.…”

Section: Discussionmentioning

confidence: 99%

Crooked tail ( Cd ) model of human folate-responsive neural tube defects is mutated in Wnt coreceptor lipoprotein receptor-related protein 6

Carter

Chen

Slowinska

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 99%

Crooked tail ( Cd ) model of human folate-responsive neural tube defects is mutated in Wnt coreceptor lipoprotein receptor-related protein 6

Carter

Chen

Slowinska

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…To begin with, growth retardation in the mutant embryos may be explained by the defects in nutrient uptake in VYS endoderm and maternal-fetal exchange. Second, defects in the uptake of small molecule nutrients such as vitamins in VYS endoderm may lead to neural tube closure defects in embryos (24,25). Megalin, an endocytic receptor for multiple ligands including the vitamin B12-transcobalamin complex (26) and the retinol-binding protein-vitamin A complex (27), is localized at the apical surface of VYS endoderm during development (13).…”

Section: Discussionmentioning

confidence: 99%

Essential role of RGS-PX1/sorting nexin 13 in mouse development and regulation of endocytosis dynamics

Zheng¹,

Tang²,

Tang

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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RGS-PX1 (also known as sorting nexin 13) is a member of both the regulator of G protein signaling (RGS) and sorting nexin (SNX) protein families. Biochemical and cell culture studies have shown that RGS-PX1͞SNX13 attenuates G␣s-mediated signaling through its RGS domain and regulates endocytic trafficking and degradation of the epidermal growth factor receptor. To understand the functions of RGS-PX1͞SNX13 in vivo, we generated mice carrying targeted mutations of Snx13 and found that systemic Snx13-null mice were embryonic lethal around midgestation. Snx13-null embryos had significant overall growth retardation and defects in neural tube closure, blood vessel formation, and the formation of the placental labyrinthine layer. Moreover, the Snx13-null visceral yolk sac endoderm cells showed dramatic changes in the organization of endocytic compartments, abundant autophagic vacuoles, and abnormal localization of several endocytic markers, including megalin, a receptor for nutrients and proteins; ARH, a coat protein that binds megalin; LAMP2; and LC3. These changes suggest that Snx13-null embryos are defective in nutrient uptake and transport, which may contribute to the other developmental abnormalities observed. Taken together, our findings demonstrate an essential role for RGS-PX1͞SNX13 in mouse development and provide previously undescribed insights into its cellular function in the regulation of endocytosis dynamics.megalin ͉ receptor endocytosis ͉ regulator of G protein signaling ͉ visceral yolk sac endoderm R eceptor-mediated endocytosis is the process by which plasma membrane components and extracellular materials such as nutrients, hormones, antigens, and other macromolecules are selectively internalized into cytoplasmic vesicles, delivered to early and late endosomes and degraded in lysosomes or recycled back to the plasma membrane through recycling endosomes (1-3). Trafficking between these endocytic compartments is highly regulated and often involves critical sorting steps. Recently, a large family of sorting nexin (SNX) proteins characterized by the presence of Phox (PX) domains has been identified and implicated in the regulation of different steps of the endocytic pathway (4, 5). For example, the founding member of the SNX family, SNX1, was identified as an interacting partner of the epidermal growth factor receptor, and overexpression of SNX1 was found to enhance lysosomal degradation of epidermal growth factor receptor (6). More recently, knock-down of SNX1 expression by RNA interference was shown to perturb the steady state distribution of the cation-independent mannose-6-phosphate receptor (CI-MPR) from the trans-Golgi network to endosomes and to increase the degradation rate of CI-MPR, establishing a role for SNX1 in endosome-to-trans-Golgi network transport (7).RGS-PX1 (also known as SNX 13, the designation by the human gene nomenclature committee) was identified originally as a member of the regulator of G protein signaling (RGS) protein family through bioinformatics analysis (8). RGS-PX1 contains...

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“…Although neural tube closure requires the coordination of a variety of cellular processes (19,20), Frem2 expression at the dorsal midline during closure suggests that the protein may act to facilitate the cellular rearrangements that occur as the neural tissue and ectoderm separate from one another and fuse to form the neural tube and its overlying ectoderm. Pigmentation defects seen in my animals are likely due to neural crest abnormalities.…”

Section: Morphogenetic Defects In My Micementioning

confidence: 99%

Tissue morphogenesis and vascular stability require the Frem2 protein, product of the mouse myelencephalic blebs gene

Timmer

Mak

Manova

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Adhesive properties of cells undergoing morphogenetic rearrangements can be regulated either at the cellular level or by altering the environment in which rearrangements occur. Here, we describe the identification of a mutation (my F11 ) in the mouse extracellular matrix component Frem2, and provide evidence that suggests Frem2 expression creates an environment conducive to morphogenetic events. Loss of Frem2 function results in defects in developmental events associated with morphogenetic rearrangements of the vasculature and of tissues arising from all germ layers. The Frem2 transcript is restricted both spatially and temporally and appears in advance of cell rearrangement events. Thus, expression of Frem2 may dynamically alter the extracellular matrix to provide a substrate for cell migration and rearrangements during embryogenesis. extracellular matrix ͉ hemorrhage ͉ Frem ͉ CALX␤ ͉ neural tube defect

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The genetic basis of mammalian neurulation

Cited by 617 publications

References 101 publications

Crooked tail ( Cd ) model of human folate-responsive neural tube defects is mutated in Wnt coreceptor lipoprotein receptor-related protein 6

Crooked tail ( Cd ) model of human folate-responsive neural tube defects is mutated in Wnt coreceptor lipoprotein receptor-related protein 6

Essential role of RGS-PX1/sorting nexin 13 in mouse development and regulation of endocytosis dynamics

Tissue morphogenesis and vascular stability require the Frem2 protein, product of the mouse myelencephalic blebs gene

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