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Irina Dulubova
Researcher at University of Texas Southwestern Medical Center
Publications - 31
Citations - 4460
Irina Dulubova is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: SNARE complex & Syntaxin. The author has an hindex of 26, co-authored 31 publications receiving 4142 citations. Previous affiliations of Irina Dulubova include Reata Pharmaceuticals & Rockefeller University.
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A conformational switch in syntaxin during exocytosis: role of munc18
Irina Dulubova,Shuzo Sugita,Sandra Hill,Masahiro Hosaka,Imma Fernandez,Thomas C. Südhof,Josep Rizo +6 more
TL;DR: The results indicate that syntaxin binds to munc18‐1 in a closed conformation and suggest that this conformation represents an essential intermediate in exocytosis, and suggest a model whereby syntaxin undergoes a large conformational switch that mediates the transition between the syntaxin–munc 18‐1 complex and the core complex.
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RIM Proteins Tether Ca2+ Channels to Presynaptic Active Zones via a Direct PDZ-Domain Interaction
Pascal S. Kaeser,Pascal S. Kaeser,Lunbin Deng,Lunbin Deng,Yun Wang,Irina Dulubova,Xinran Liu,Josep Rizo,Thomas C. Südhof +8 more
TL;DR: It is proposed that RIMs tether N- and P/Q-type Ca(2+) channels to presynaptic active zones via a direct PDZ-domain-mediated interaction, thereby enabling fast, synchronous triggering of neurotransmitter release at a synapse.
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Munc18-1 binds directly to the neuronal SNARE complex
TL;DR: The results suggest that binding of Munc18-1 to closed syntaxin-1 is a specialization that evolved to meet the strict regulatory requirements of neuronal exocytosis, whereas binding of munc18 -1 to assembled SNARE complexes reflects a general function of SM proteins involved in executing membrane fusion.
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Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.
TL;DR: NMR spectroscopy is used to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure, indicating a specific role in exocytosis.
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Conformational Switch of Syntaxin-1 Controls Synaptic Vesicle Fusion
Stefan H. Gerber,Jong-Cheol Rah,Jong-Cheol Rah,Sang-Won Min,Xinran Liu,Heidi de Wit,Irina Dulubova,Alexander C. Meyer,Josep Rizo,Marife Arancillo,Robert E. Hammer,Matthijs Verhage,Christian Rosenmund,Christian Rosenmund,Thomas C. Südhof +14 more
TL;DR: During synaptic vesicle fusion, the soluble N-ethylmaleimide-sensitive factor–attachment protein receptor (SNARE) protein syntaxin-1 exhibits two conformations that both bind to Munc18-1: a “closed” conformation outside the SNARE complex and an “open’ conformation in theSNARE complex.