有哪些信誉好的足球投注网站antagonism of lin-17frizzled and lin-18ryk in nematode vulva induction reveals evolutionary alterations in core developmental pathwayslin-17frizzled和lin-18ryk拮抗线虫阴户感应揭示进化改变核心发展途径.pdfVIP
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antagonism of lin-17frizzled and lin-18ryk in nematode vulva induction reveals evolutionary alterations in core developmental pathwayslin-17frizzled和lin-18ryk拮抗线虫阴户感应揭示进化改变核心发展途径
Antagonism of LIN-17/Frizzled and LIN-18/Ryk in
Nematode Vulva Induction Reveals Evolutionary
Alterations in Core Developmental Pathways
Xiaoyue Wang, Ralf J. Sommer*
¨
Department for Evolutionary Biology, Max-Planck Institut for Developmental Biology, Tubingen, Germany
Abstract
Most diversity in animals and plants results from the modification of already existing structures. Many organ systems, for
example, are permanently modified during evolution to create developmental and morphological diversity, but little is
known about the evolution of the underlying developmental mechanisms. The theory of developmental systems drift
proposes that the development of conserved morphological structures can involve large-scale modifications in their
regulatory mechanisms. We test this hypothesis by comparing vulva induction in two genetically tractable nematodes,
Caenorhabditis elegans and Pristionchus pacificus. Previous work indicated that the vulva is induced by epidermal growth
factor (EGF)/RAS and WNT signaling in Caenorhabditis and Pristionchus, respectively. Here, we show that the evolution of
vulva induction involves major molecular alterations and that this shift of signaling pathways involves a novel wiring of WNT
signaling and the acquisition of novel domains in otherwise conserved receptors in Pristionchus vulva induction. First, Ppa-
LIN-17/Frizzled acts as an antagonist of WNT signaling and suppresses the ligand Ppa-EGL-20 by ligand sequestration.
Second, Ppa-LIN-18/Ryk transmits WNT signaling and requires inhibitory SH3 domain binding motifs, unknown from Cel-LIN-
18/Ryk. Third, Ppa-LIN-18/Ryk signaling involves Axin and b-catenin and Ppa-axl-1/Axin is epistatic to Ppa-lin-18/Ryk. These
resul
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