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Wei Sun Park

Researcher at KAIST

Publications -  21
Citations -  2083

Wei Sun Park is an academic researcher from KAIST. The author has contributed to research in topics: Rab & Endosome. The author has an hindex of 12, co-authored 17 publications receiving 1907 citations. Previous affiliations of Wei Sun Park include California Institute of Technology & Stanford University.

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Journal ArticleDOI

PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane.

TL;DR: This work surveyed PM-targeting mechanisms by imaging the subcellular localization of 125 fluorescent protein–conjugated Ras, Rab, Arf, and Rho proteins and found that proteins with polybasic clusters dissociated from the PM only when both PI(4,5)P2 and phosphatidylinositol 3,4, 5-trisphosphate were depleted.
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STIM2 Is a Feedback Regulator that Stabilizes Basal Cytosolic and Endoplasmic Reticulum Ca2+ Levels

TL;DR: An siRNA screen of the human signaling proteome is performed to identify regulators of basal Ca2+ concentration and found STIM2 as the strongest positive regulator and places it at the center of a feedback module that keeps basal cytosolic and ER Ca2- concentrations within tight limits.
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Cooperative activation of PI3K by Ras and Rho family small GTPases.

TL;DR: A distributed network of Ras and Rho family small GTPases induces and reinforces PI3K activity, explaining past challenges to elucidate the specific relevance of different small G TPases in regulatingPI3K and controlling cell polarization and chemotaxis.
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Comprehensive identification of PIP3-regulated PH domains from C elegans to H sapiens by model prediction and live imaging

TL;DR: A recursive-learning algorithm was developed and validated that it accurately predicts PIP3 regulation and showed that PIP2 regulation is specified by amino acids across the PH domain, not just the Pip3-binding pocket, and must have evolved several times independently from P IP3-insensitive ancestral PH domains.
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VipD of Legionella pneumophila Targets Activated Rab5 and Rab22 to Interfere with Endosomal Trafficking in Macrophages

TL;DR: The crystal structure of VipD of L. pneumophila is reported and it is shown that its C-terminal domain robustly interferes with endosomal trafficking through tight and selective interactions with Rab5 and Rab22.