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Type |
Poster Presentation |
Area |
Life Chemistry |
Room No. |
Event Hall |
Time |
4월 20일 (금요일) 11:00~12:30 |
Code |
BIO.P-287 |
Subject |
Actin polymerization inside Giant Unilamellar Vesicles |
Authors |
Mary Chuong, Kwanwoo Shin* Department of Chemistry, Sogang University, Korea |
Abstract |
Globular actin (G actin) is the most abundant protein found in most eukaryotic cells. It is involved in various cellular phenomena such as cell division, cell motility, cell shape, and cell growth. These actins are activated by ATP to formed actin in fiber formed, but this state is very unstable and easily broken by fluid flow. Therefore, to handle actin in laboratory, ions like K+ and Mg2+ were used in this study. Our goal was to make actin polymerization inside artificial vesicles, known as Giant Unilamellar Vesicles (GUVs). These phospholipids constituting vesicles were accompanied by ionophores (K+ and Mg2+) and fabricated using electroformation technique. Rabbit Skeletal Muscle Actin were used with the addition of Amanita phalloides, ATP, and Ca2+. Then the actin polymerization was performed by slowly adding polymerization buffer containing KCl and MgCl into the vesicles and observed on confocal microscope.
References
1. Dominguez, R., & Holmes, K. C. (2011). Actin Structure and Function. Annual Review of Biophysics, 40, 169–186.
2. Olson, E. N., & Nordheim, A. (2010). Linking actin dynamics and gene transcription to drive cellular motile functions. Nature Reviews. Molecular Cell Biology, 11(5), 353–365.
3. Polymerization of actin by positively charged liposomes. (1988). The Journal of Cell Biology, 106(4), 1221–1227.
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E-mail |
marychuong05@gmail.com |
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