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Hye-Won Shin

Researcher at Kyoto University

Publications -  66
Citations -  3240

Hye-Won Shin is an academic researcher from Kyoto University. The author has contributed to research in topics: Endosome & Golgi apparatus. The author has an hindex of 31, co-authored 62 publications receiving 2857 citations. Previous affiliations of Hye-Won Shin include Tohoku University & University of Tsukuba.

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An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway

TL;DR: The data provide the first evidence for a dual role of a Rab GTPase in regulating both generation and turnover of PIs via PI kinases and phosphatases to coordinate signaling functions with organelle homeostasis.
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Rab11 regulates exocytosis of recycling vesicles at the plasma membrane

TL;DR: In addition to its role in recycling processes at perinuclear recycling endosomes, Rab11 is transported along microtubules to the cell periphery through association with recycling carriers, and directly regulates vesicle exocytosis at the plasma membrane in concert with the exocyst.
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BIG2, A Guanine Nucleotide Exchange Factor for ADP-Ribosylation Factors: Its Localization to Recycling Endosomes and Implication in the Endosome Integrity

TL;DR: It is shown that BIG2 has an exchange activity toward class I ARFs (ARF1 and ARF3) in vivo and inactivation of either ARF exaggerates the BIG2(E738K)-induced tubulation of endosomal membranes, indicating that BIG1 is implicated in the structural integrity of the recycling endosome through activating class IARFs.
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Identification and Subcellular Localization of a Novel Mammalian Dynamin-Related Protein Homologous to Yeast Vps1p and Dnm1p

TL;DR: Immunofluorescence analysis of cells expressing epitope-tagged DVLP revealed that it showed a diffused perinuclear staining pattern that was not superimposed on that of the marker protein for the Golgi apparatus, trans-Golgi network, lysosomes, endosome, or endoplasmic reticulum, suggesting that DVLP is not involved in the formation of known coated vesicles.
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Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1.

TL;DR: The C-terminal binding regions of FIP3 and FIP4 for Rab11 and ARF5/ARF6 are defined and the crystal structure of Rab11 in complex with the Rab11-binding domain (RBD) of F IP3 is determined.