OAK

Elucidating the Role of ALK2-ALK1 Heterodimer in Endothelial Cells

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Abstract
The BMP signaling pathway is a signaling cascade that involves phosphorylation of serine/threonine residues. The conventional BMP signaling pathway is generally described as the activation of dimeric type II BMP receptors upon induction by dimeric BMP ligands, leading to the phosphorylation of dimeric type I BMP receptors. The structural arrangement of the heterotetrameric receptor complex enables signal transduction. However, recent studies have consistently suggested the possibility of not only homodimer formation but also heteromeric complexes by BMP receptor dimerization. These studies imply the conventional BMP signaling of receptor dimerization exclusively leads to diverse heterotetrameric complex formation of signal transduction, suggesting a need to reinterpret the BMP signaling pathway with the possibility of various receptor oligomerization mechanisms.
The BMP signaling pathway regulates the angiogenesis and differentiation of endothelial cells. Using a mouse retina model, different BMPR1s demonstrate control opposing function of vascular development. In this research, we aimed that investigate the potential formation of heteromeric complexes among type I receptors in endothelial cells and how the binding preferences change depending on ligands. When BMP Type I receptors were overexpressed in endothelial cells to determine their preferred interactions. Additionally, human disease mutations of ALK2 various at different positions which alter receptor function prefer to form a homodimer of BMPR1s possible to form a heterodimer complete with Type II BMP receptors was examined. In conclusion, the formation of ALK2 homodimer for signal transduction is unlikely in HUVEC. Instead, ALK2 predominantly forms heteromeric complexes with ALK1 or ALK3. This suggests a potential mechanism for regulation, where ALK2 functions as a modulator by binding to ALK1 or ALK3 to form heteromeric complexes rather than acting as a conventional homodimer complex for signal transduction.
Author(s)
Heewon Cho
Issued Date
2023
Type
Thesis
URI
https://scholar.gist.ac.kr/handle/local/19236
Alternative Author(s)
조희원
Department
대학원 생명과학부
Advisor
Jin, Suk-Won
Degree
Master
Appears in Collections:
Department of Life Sciences > 3. Theses(Master)
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