THESIS
2016
xvi, 114 pages : illustrations (some color) ; 30 cm
Abstract
The Bone Morphogenetic Protein (BMP) Signaling Pathway is evolutionarily conserved with
significant roles in regulations of multiple developmental processes. Its regulation is achieved
by modulation of the BMP ligand availability and the receptor relay molecules activities
targeting downstream gene regulation. This conserved BMP signaling pathway, a.k.a., the
Sma/Mab pathway in C. elegans, plays a significant role in the body length regulation. To
understand the extracellular regulation of the Sma/Mab signaling, this study focused on
sma-10, a gene encoding a leucine-rich repeats and immunoglobulin-like domains protein that
enhances the Sma/Mab signal. My work aimed to understand expression profile of sma-10, to
identify the required protein domains of SMA-10 for Sma/Mab signali...[
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The Bone Morphogenetic Protein (BMP) Signaling Pathway is evolutionarily conserved with
significant roles in regulations of multiple developmental processes. Its regulation is achieved
by modulation of the BMP ligand availability and the receptor relay molecules activities
targeting downstream gene regulation. This conserved BMP signaling pathway, a.k.a., the
Sma/Mab pathway in C. elegans, plays a significant role in the body length regulation. To
understand the extracellular regulation of the Sma/Mab signaling, this study focused on
sma-10, a gene encoding a leucine-rich repeats and immunoglobulin-like domains protein that
enhances the Sma/Mab signal. My work aimed to understand expression profile of sma-10, to
identify the required protein domains of SMA-10 for Sma/Mab signaling modulation and to
elucidate the impact of SMA-10 on SMA-6/DAF-4 receptor complex trafficking. We revealed
that sma-10 is constitutively expressed in the pharynx, intestine and hypodermis at steady
levels throughout the larval development. All the extracellular domains of SMA-10 are
required while membrane anchorage is dispensable for its functionality. We have further
identified large SMA-6 containing intracellular vesicles in the intestinal cells of sma-10
mutant, suggesting a potential linkage between the Sma/Mab regulation and the intracellular
trafficking of Type I BMP receptor regulated by SMA-10.
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