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Junichi Yuasa-Kawada

Researcher at Fukuoka University

Publications -  9
Citations -  216

Junichi Yuasa-Kawada is an academic researcher from Fukuoka University. The author has contributed to research in topics: Slit & Axon guidance. The author has an hindex of 5, co-authored 9 publications receiving 176 citations. Previous affiliations of Junichi Yuasa-Kawada include Northwestern University & Okinawa Institute of Science and Technology.

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Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in inhibiting breast cancer cell migration

TL;DR: It is shown that ubiquitin-specific protease 33 (USP33)/VDU1, originally identified as a von Hippel–Lindau tumor suppressor (VHL) protein-interacting deubiquitinating enzyme, binds to the Robo1 receptor, and that USP33 is required for Slit responsiveness in breast cancer cells.
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Midline crossing and Slit responsiveness of commissural axons require USP33

TL;DR: This work found that the deubiquitinating enzyme USP33 interacts with the Robo1 receptor, revealing a previously unknown role for USP 33 in vertebrate commissural axon guidance and in Slit signaling.
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A crucial role for Arf6 in the response of commissural axons to Slit

TL;DR: It is found that a Robo1 endocytosis-triggered and Arf6-mediated positive-feedback strengthens the Slit response in commissural axons upon their midline crossing and provides insights into endocytic trafficking-mediated mechanisms for spatiotemporally controlled axonal responses.
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The BH3-Only SNARE BNip1 Mediates Photoreceptor Apoptosis in Response to Vesicular Fusion Defects

TL;DR: It is reported that photoreceptors undergo apoptosis in a zebrafish β-soluble N-ethylmaleimide-sensitive factor attachment protein (β-SNAP) mutant and that BNip1 transforms vesicular fusion defects into photoreceptor apoptosis, suggesting that the syntaxin-18 cis-SNARE complex functions as an alarm factor that monitors vesicle fusion competence.
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Dctn1 binds to tdp-43 and regulates tdp-43 aggregation

TL;DR: In this paper, the authors used a panel of truncated mutants to identify a new player in TDP-43 cytoplasmic-nuclear transport, and showed that dysregulation of DCTN1-TDP43 interactions triggers mislocalization and aggregation of TDP43, thus providing insights into the pathological mechanisms of Perry disease.