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Mad Linker Phosphorylations Regulates BMP Type I Receptor Turnover in Drosophila
Başlık:
Mad Linker Phosphorylations Regulates BMP Type I Receptor Turnover in Drosophila
Yazar:
Urrutia, Hugo Alexander, author.
ISBN:
9780438069985
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (33 pages)
Genel Not:
Source: Masters Abstracts International, Volume: 57-06M(E).
Advisors: Edward V. Eivers Committee members: Nathan J. Lanning; Robert Nissen.
Özet:
Deciphering how signaling pathways are regulated is essential for biologists to understand the role these cellular events play during development. Embryonic patterning is regulated by growth factor gradients, and cells must interpret these gradients to accomplish precise developmental management. The Eivers' lab is currently investigating how a phospho-serine code in the central/linker domain of the Bone Morphogenetic Protein (BMP) transcription factor Mad modulates this signaling cascade in developing Drosophila tissues. Previous work has determined that phosphorylation of serines 212, 208, and 204 in the linker domain of Mad, by Cyclin-dependent kinase 8 and Shaggy, play an essential role in controlling the duration and range of BMP signaling in embryonic tissues and result in signal termination via Mad degradation. My research set out to determine if Mad linker phosphorylation modulated the intensity and duration of BMP signaling beyond proteasomal degradation of Mad. More specifically, I was interested if linker phosphorylated Mad might play a role in degradation of the endocytosed BMP receptor, Thickveins. My work uncovered that linker phosphorylated Mad localized to distinct cellular puncta along the developing pupal wing margin. Interestingly, a number of these puncta co-localized with the endocytosed BMP receptor, Thickveins. Chemical inhibition of the proteasome lead to the stabilization of Thickveins protein, while lysosomal inhibition did not result in stabilization of the BMP receptor. Finally, expression of Mad linker mutants in S2 cells resulted in moderate stabilization of Thickveins. My findings raise the potential that linker phosphorylated Mad might be a critical signal to direct a specific subpopulation of endocytosed Thickveins to proteasomes, thus adding a new layer of regulation to this signaling cascade.
Notlar:
School code: 0962
Tüzel Kişi Ek Girişi:
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Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(692629.1) | 692629-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
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