Results 1 to 10 of about 26,023 (249)

SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18

eLife, 2014
Secretory and endolysosomal fusion events are driven by SNAREs and cofactors, including Sec17/α-SNAP, Sec18/NSF, and Sec1/Munc18 (SM) proteins. SMs are essential for fusion in vivo, but the basis of this requirement is enigmatic.
Braden T Lobingier, Daniel P Nickerson, Sheng-Ying Lo, Alexey J Merz   +3 more
doaj   +1 more source

Fluorescence Lifetime Imaging Microscopy reveals rerouting of SNARE trafficking driving dendritic cell activation

eLife, 2017
SNARE proteins play a crucial role in intracellular trafficking by catalyzing membrane fusion, but assigning SNAREs to specific intracellular transport routes is challenging with current techniques.
Daniëlle Rianne José Verboogen, Natalia González Mancha, Martin ter Beest, Geert van den Bogaart   +3 more
doaj   +1 more source

Synergistic actions of v-SNARE transmembrane domains and membrane-curvature modifying lipids in neurotransmitter release

eLife, 2020
Vesicle fusion is mediated by assembly of SNARE proteins between opposing membranes. While previous work suggested an active role of SNARE transmembrane domains (TMDs) in promoting membrane merger (Dhara et al., 2016), the underlying mechanism remained ...
Madhurima Dhara, Maria Mantero Martinez, Mazen Makke, Yvonne Schwarz, Ralf Mohrmann, Dieter Bruns   +5 more
doaj   +1 more source

Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion

Nature Communications, 2017
Membrane fusion during exocytosis is mediated by interaction between SNARE proteins on vesicles and the cell membrane, but how SNARE complex assembly is initiated remains unknown.
Peng Yue, Yubo Zhang, Kunrong Mei, Shaoxiao Wang, Johannes Lesigang, Yueyao Zhu, Gang Dong, Wei Guo   +7 more
doaj   +1 more source

Ultrastructure and immunohistochemical characterization of proteins concerned with the secretory machinery in goat ceruminous glands

European Journal of Histochemistry, 2017
The expression of soluble N-ethyl-maleimide sensitive fusion attachment protein receptor (SNARE) proteins in apocrine glands has not been fully elucidated. In addition to performing ultrastructural observation of the ceruminous glands in goats, our study
Tadashi Yasui, Hiroshi Gomi, Taishi Kitahara, Azuma Tsukise   +3 more
doaj   +1 more source

VAMP-2, SNAP-25A/B and syntaxin-1 in glutamatergic and GABAergic synapses of the rat cerebellar cortex

BMC Neuroscience, 2011
Background The aim of this study was to assess the distribution of key SNARE proteins in glutamatergic and GABAergic synapses of the adult rat cerebellar cortex using light microscopy immunohistochemical techniques.
Benagiano Vincenzo, Lorusso Loredana, Flace Paolo, Girolamo Francesco, Rizzi Anna, Bosco Lorenzo, Cagiano Raffaele, Nico Beatrice, Ribatti Domenico, Ambrosi Glauco   +9 more
doaj   +1 more source

Single-molecule two- and three-colour FRET studies reveal a transition state in SNARE disassembly by NSF

Nature Communications
SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptor) proteins are the minimal machinery required for vesicle fusion in eukaryotes. Formation of a highly stable four-helix bundle consisting of SNARE motif of these proteins, drives
Sudheer K. Cheppali, Chang Li, Wenjing Xing, Ruirui Sun, Mengyi Yang, Yi Xue, Si-Yao Lu, Jun Yao, Shan Sun, Chunlai Chen, Sen-Fang Sui   +10 more
doaj   +1 more source

Lateral Fluid Percussion Injury Impairs Hippocampal Synaptic Soluble N-Ethylmaleimide Sensitive Factor Attachment Protein Receptor Complex Formation

Frontiers in Neurology, 2017
Traumatic brain injury (TBI) and the activation of secondary injury mechanisms have been linked to impaired cognitive function, which, as observed in TBI patients and animal models, can persist for months and years following the initial injury ...
Shaun W. Carlson, Shaun W. Carlson, Jeremy Henchir, Jeremy Henchir, C. Edward Dixon, C. Edward Dixon   +5 more
doaj   +1 more source

Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site

Nature Communications
The regulated release of chemical messengers is crucial for cell-to-cell communication; abnormalities in which impact coordinated human body function. During vesicular secretion, multiple SNARE complexes assemble at the release site, leading to fusion ...
Bhavya R. Bhaskar, Laxmi Yadav, Malavika Sriram, Kinjal Sanghrajka, Mayank Gupta, Boby K. V, Rohith K. Nellikka, Debasis Das   +7 more
doaj   +1 more source

Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE

Cell Reports, 2019
Summary: Intracellular vesicle fusion is mediated by soluble N-ethylmaleimide sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18 (SM) proteins. It is generally accepted that membrane fusion occurs when the vesicle and target membranes
Shailendra S. Rathore, Yinghui Liu, Haijia Yu, Chun Wan, MyeongSeon Lee, Qian Yin, Michael H.B. Stowell, Jingshi Shen   +7 more
doaj   +1 more source