Seong Joo Koo
Leibniz Institute for Neurobiology
13 Papers
65 Citations
Seong Joo Koo is an academic researcher from Leibniz Institute for Neurobiology. The author has contributed to research in topics: Endocytic cycle & Synaptic vesicle. The author has an hindex of 8, co-authored 10 publications. Previous affiliations of Seong Joo Koo include Leibniz Association & Free University of Berlin.
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Papers
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins
Benjamin G. Wilhelm,Sunit Mandad,Sven Truckenbrodt,Katharina Kröhnert,Christina Schäfer,Burkhard Rammner,Seong Joo Koo,Gala A. Claßen,Michael Krauss,Volker Haucke,Henning Urlaub,Henning Urlaub,Silvio O. Rizzoli +12 more
TL;DR: A quantitative molecular-scale image of the “average” synapse populated with realistic renditions of each of the protein components that contribute to the inner workings of neurons is presented, displaying 300,000 proteins in atomic detail.
Vesicular Synaptobrevin/VAMP2 Levels Guarded by AP180 Control Efficient Neurotransmission
Seong Joo Koo,Gaga Kochlamazashvili,Benjamin R. Rost,Dmytro Puchkov,Niclas Gimber,Martin Lehmann,Martin Lehmann,Georgi Tadeus,Jan Schmoranzer,Jan Schmoranzer,Christian Rosenmund,Volker Haucke,Volker Haucke,Volker Haucke,Tanja Maritzen +14 more
TL;DR: It is demonstrated that loss of the Syb 2-specific endocytic adaptor AP180 causes a moderate activity-dependent reduction of vesicular Syb2 levels, defects in SV reformation, and a corresponding impairment of neurotransmission that lead to excitatory/inhibitory imbalance, epileptic seizures, and premature death.
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CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process.
Alessandra Granata,Seong Joo Koo,Volker Haucke,Volker Haucke,Giampietro Schiavo,Thomas T. Warner +5 more
TL;DR: Retrieval of surface‐stranded synaptotagmin 1 is restored by overexpression of stonin 2 in ΔE‐TA‐expressing cells, suggesting that the DYT1 mutation compromises the role of TA in protein stabilisation and synaptic vesicle recycling.
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Turning CALM into excitement: AP180 and CALM in endocytosis and disease.
TL;DR: The current state of knowledge about the roles of AP180 and CALM family members in clathrin‐dependent membrane traffic, the molecular mechanistic basis for their activities and their potential involvement in human disease are summarized.
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Proteomic discovery of chemical probes that perturb protein complexes in human cells
Michael R. Lazear,Jarrett R. Remsberg,Martin G. Jaeger,Katie Rothamel,Hsuan-lin Her,Kristen E. DeMeester,Evert Njomen,Simon J. Hogg,J. Rahman,Landon R. Whitby,Sang Joon Won,Michael A. Schafroth,Daisuke Ogasawara,Minoru Yokoyama,Garrett L. Lindsey,Haoxin Li,Jason Germain,Sabrina Barbas,Joan Vaughan,Thomas W. Hanigan,Vincent F. Vartabedian,Christopher J. Reinhardt,Melissa M. Dix,Seong Joo Koo,In-Sook Heo,John R. Teijaro,Gabriel M. Simon,Brahma Ghosh,Omar Abdel-Wahab,Kay Ahn,Alan Saghatelian,Bruno Melillo,Stuart L. Schreiber,Gene W. Yeo,Benjamin F. Cravatt +34 more
TL;DR: In this paper, a function-first proteomic strategy that uses size exclusion chromatography (SEC) to assess the global impact of electrophilic compounds on protein complexes in human cells is described.
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