Results 11 to 20 of about 176,593 (250)

Coarse‐Grain Simulations of the R‐SNARE Fusion Protein in its Membrane Environment Detect Long‐Lived Conformational Sub‐States

ChemPhysChem, 2009
AbstractThe detected conformational sub‐states of an R‐SNARE peptide inserted in a lipid bilayer (see figure) give insights into the membrane fusion mechanism. The simulations are in agreement with most experimental data on the SNARE system, but differ in some details that may have a functional interest.
Durrieu, Marie-Pierre, Bond, Peter, Sansom, Mark, Lavery, Richard, Baaden, Marc   +4 more
openaire   +5 more sources

Longin R-SNARE is retrieved from the plasma membrane by ANTH domain-containing proteins inArabidopsis

Proceedings of the National Academy of Sciences, 2020
SignificanceThe plasma membrane (PM) acts as the interface between intra- and extracellular environments and is thus important for intercellular communication and extracellular signal perception. The composition and amounts of PM proteins are tightly regulated, by molecular mechanisms that remain largely unknown in plant cells.
Masaru Fujimoto, Kazuo Ebine, Kohji Nishimura, Nobuhiro Tsutsumi, Takashi Ueda   +4 more
openaire   +2 more sources

Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments [PDF]

Proceedings of the National Academy of Sciences, 2019
Significance Although each intracellular fusion event is catalyzed by similar proteins, organelle-specific fusion is essential for accurate protein compartmentation. Prior studies have suggested that specificity resides in the SNARE proteins or in SNAREs and their Sec1/Munc18 (SM) chaperones.
Youngsoo Jun, William Wickner
openaire   +2 more sources

The Sec1/Munc18 protein Vps45 regulates cellular levels of its SNARE binding partners Tlg2 and Snc2 in Saccharomyces cerevisiae [PDF]

, 2012
Intracellular membrane trafficking pathways must be tightly regulated to ensure proper functioning of all eukaryotic cells. Central to membrane trafficking is the formation of specific SNARE (soluble N-ethylmeleimide-sensitive factor attachment protein ...
Marion S Struthers, Nia J Bryant, Lindsay N Carpp, Carpp Lindsay N., Shanks, S.G., McCann Rebecca K., Carpp, L.N., Struthers, M.S., Bryant, N.J., Scott G Shanks, Struthers Marion S., McCann, R.K., Bryant Nia J., Hong, W., Shanks Scott G., Rebecca K McCann   +15 more
core   +1 more source

Comparative analysis of plant genomes allows the definition of the "Phytolongins": a novel non-SNARE longin domain protein family

BMC Genomics, 2009
Background Subcellular trafficking is a hallmark of eukaryotic cells. Because of their pivotal role in the process, a great deal of attention has been paid to the SNARE proteins.
Dacks Joel B, Rossi Valeria, Vedovato Marco, Filippini Francesco   +3 more
doaj   +1 more source

Secretory vesicles are preferentially targeted to areas of low molecular SNARE density [PDF]

, 2012
Intercellular communication is commonly mediated by the regulated fusion, or exocytosis, of vesicles with the cell surface. SNARE (soluble N-ethymaleimide sensitive factor attachment protein receptor) proteins are the catalytic core of the secretory ...
Weiping Lu (120665), Dun, Alison R., Lu, Weiping, Rory R. Duncan (120667), Weiping Lu, Gabriel J. Lord (120664), Colin Rickman (120669), Andrew Dunn, Gabriel J Lord, Martin, Kirsty J, Lei Yang (102719), Qiu, Zhen, Rickman, Colin; id_orcid, Kirsty J Martin, Lei Yang, Duncan, Rory R, Duncan, Rory R., Alison R. Dun (120660), Zhen Qiu (120662), Rickman, Colin, Dun, Alison, Qiu, Zhen; id_orcid, Colin Rickman, Rory R Duncan, Lord, Gabriel J, Kirsty J. Martin (120661), Alison R Dun, Lord, Gabriel J., Yang, Lei, Martin, Kirsty J., Andrew Dunn (120663), Dunn, Andrew, Zhen Qiu   +32 more
core   +1 more source

Negative regulation of syntaxin4/SNAP-23/VAMP2-mediated membrane fusion by Munc18c In Vitro [PDF]

, 2008
Background: Translocation of the facilitative glucose transporter GLUT4 from an intracellular store to the plasma membrane is responsible for the increased rate of glucose transport into fat and muscle cells in response to insulin.
Nia J Bryant, Gould, G.W., Veronica Aran, James A McNew, Gwyn W Gould, McNew, J.A., Bryant, N.J., Aran Veronica, Avani Verma, Gould Gwyn W., Aran-Ponte, V., Fiona M Brandie, Bryant Nia J., Verma Avani, Brandie Fiona M., McNew James A., Brandie, F.M., Verma, A.   +17 more
core   +1 more source

ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat [PDF]

, 2002
In eukaryotic cells, secretion is achieved by vesicular transport. Fusion of such vesicles with the correct target compartment relies on SNARE proteins on both vesicle (v-SNARE) and the target membranes (t-SNARE).
Rein, U., Rein, Ulrike, Anne Spang, Spang, Anne, Hans Dieter Schmitt, Andag, Uwe, Ulrike Rein, Duden, R., Schmitt, Hans Dieter, Duden, Rainer, Spang, A., Andag, U., Uwe Andag, Schmitt, H. D., Rainer Duden, Schmitt, H.   +15 more
core   +1 more source

The Arabidopsis R-SNARE VAMP714 is essential for polarization of PIN proteins in the establishment and maintenance of auxin gradients [PDF]

, 2019
Summary The plant hormone auxin and its directional intercellular transport plays a major role in diverse aspects of plant growth and development. The establishment of auxin gradients in plants requires asymmetric distribution of members of the auxin efflux carrier PIN ...
Xiaoyan Gu, Kumari Fonseka, Stuart A. Casson, Andrei Smertenko, Guangqin Guo, Jennifer F. Topping, Patrick J. Hussey, Keith Lindsey   +7 more
openaire   +1 more source

Regional and developmental brain expression patterns of SNAP25 splice variants [PDF]

, 2011
SNAP25 is an essential SNARE protein for regulated exocytosis in neuronal cells. Differential splicing of the SNAP25 gene results in the expression of two transcripts, SNAP25a and SNAP25b.
Chamberlain, Luke H., Chamberlain Luke H, Prescott, Gerald R, Prescott Gerald R, Luke H Chamberlain, Prescott, Gerald R., Gerald R Prescott, Chamberlain, Luke H   +7 more
core   +1 more source