scholarly journals A Method to Rapidly Induce Organelle-Specific Molecular Activities and Membrane Tethering

2014 ◽  
pp. 231-245 ◽  
Author(s):  
Toru Komatsu ◽  
Takanari Inoue
Keyword(s):  
Membrane Tethering

Lipid Raft-Mediated Membrane Tethering and Delivery of Hydrophobic Cargos from Liquid Crystal-Based Nanocarriers

2016 ◽  
Vol 27 (4) ◽  
pp. 982-993 ◽  
Author(s):  
Okhil K. Nag ◽  
Jawad Naciri ◽  
Eunkeu Oh ◽  
Christopher M. Spillmann ◽  
James B. Delehanty
Keyword(s):  
Liquid Crystal ◽  
Lipid Raft ◽  
Membrane Tethering

scholarly journals Membrane-anchored human Rab GTPases directly mediate membrane tethering in vitro

Biology Open ◽  
2014 ◽  
Vol 3 (11) ◽  
pp. 1108-1115 ◽  
Author(s):  
N. Tamura ◽  
J. Mima
Keyword(s):  
Rab Gtpases ◽  
Membrane Tethering

scholarly journals Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion

2015 ◽  
Vol 26 (2) ◽  
pp. 305-315 ◽  
Author(s):  
Amy Orr ◽  
William Wickner ◽  
Scott F. Rusin ◽  
Arminja N. Kettenbach ◽  
Michael Zick
Keyword(s):  
Protein Sorting ◽  
Rab Gtpase ◽  
Attachment Protein ◽  
Functional Relationships ◽  
Sensitive Factor ◽  
Protein Receptors ◽  
Membrane Tethering ◽  
Rab Effector ◽  
Supporting Membrane ◽  
Acidic Lipids

Fusion of yeast vacuoles requires the Rab GTPase Ypt7p, four SNAREs (soluble N-ethylmaleimide–sensitive factor attachment protein receptors), the SNARE disassembly chaperones Sec17p/Sec18p, vacuolar lipids, and the Rab-effector complex HOPS (homotypic fusion and vacuole protein sorting). Two HOPS subunits have direct affinity for Ypt7p. Although vacuolar fusion has been reconstituted with purified components, the functional relationships between individual lipids and Ypt7p:GTP have remained unclear. We now report that acidic lipids function with Ypt7p as coreceptors for HOPS, supporting membrane tethering and fusion. After phosphorylation by the vacuolar kinase Yck3p, phospho-HOPS needs both Ypt7p:GTP and acidic lipids to support fusion.

scholarly journals Structure of the Membrane-tethering GRASP Domain Reveals a Unique PDZ Ligand Interaction That Mediates Golgi Biogenesis

2011 ◽  
Vol 286 (23) ◽  
pp. 20125-20129 ◽  
Author(s):  
Steven T. Truschel ◽  
Debrup Sengupta ◽  
Adam Foote ◽  
Annie Heroux ◽  
Mark R. Macbeth ◽  
...  
Keyword(s):  
Ligand Interaction ◽  
Membrane Tethering

Synbindin restrains proinflammatory macrophage activation against microbiota and mucosal inflammation during colitis

Gut ◽  
2021 ◽  
pp. gutjnl-2020-321094
Author(s):  
Luoyan Ai ◽  
Yimeng Ren ◽  
Mingming Zhu ◽  
Shiyuan Lu ◽  
Yun Qian ◽  
...  
Keyword(s):  
Macrophage Activation ◽  
Intestinal Inflammation ◽  
Fusobacterium Nucleatum ◽  
Degradation Pathway ◽  
Mucosal Inflammation ◽  
Intestinal Epithelial ◽  
Heterozygous Deletion ◽  
Macrophage Response ◽  
Dss Colitis ◽  
Membrane Tethering

ObjectiveAs a canonical membrane tethering factor, the function of synbindin has been expanding and indicated in immune response. Here, we investigated the role of synbindin in the regulation of toll-like receptor 4 (TLR4) signalling and macrophage response to microbiota during colitis.DesignThree distinct mouse models allowing global, myeloid-specific or intestinal epithelial cell-specific synbindin heterozygous deletion were constructed and applied to reveal the function of synbindin during dextran sodium sulfate (DSS) colitis. Effects of synbindin on TLR4 signalling and macrophage activation in response to bacterial lipopolysaccharide (LPS) or Fusobacterium nucleatum were evaluated. The colocalisation and interaction between synbindin and Rab7b were determined by immunofluorescence and coimmunoprecipitation. Synbindin expression in circulating monocytes and intestinal mucosal macrophages of patients with active IBD was detected.ResultsGlobal synbindin haploinsufficiency greatly exacerbated DSS-induced intestinal inflammation. The increased susceptibility to DSS was abolished by gut microbiota depletion, while phenocopied by specific synbindin heterozygous deletion in myeloid cells rather than intestinal epithelial cells. Profoundly aberrant proinflammatory gene signatures and excessive TLR4 signalling were observed in macrophages with synbindin interference in response to bacterial LPS or Fusobacterium nucleatum. Synbindin was significantly increased in intestinal mucosal macrophages and circulating monocytes from both mice with DSS colitis and patients with active IBD. Interleukin 23 and granulocyte-macrophage colony-stimulating factor were identified to induce synbindin expression. Mechanistic characterisation indicated that synbindin colocalised and directly interacted with Rab7b, which coordinated the endosomal degradation pathway of TLR4 for signalling termination.ConclusionSynbindin was a key regulator of TLR4 signalling and restrained the proinflammatory macrophage activation against microbiota during colitis.

p97 and p47 function in membrane tethering in cooperation with FTCD during mitotic Golgi reassembly

2021 ◽  
Author(s):  
Yayoi Kaneko ◽  
Kyohei Shimoda ◽  
Rafael Ayala ◽  
Yukina Goto ◽  
Silvia Panico ◽  
...  
Keyword(s):  
Membrane Tethering

scholarly journals The endoplasmic reticulum-plasma membrane tethering protein TMEM24 is a regulator of cellular Ca2+ homeostasis

2021 ◽  
Author(s):  
Beichen Xie ◽  
Styliani Panagiotou ◽  
Jing Cen ◽  
Patrick Gilon ◽  
Peter Bergsten ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Insulin Secretion ◽  
Lipid Transfer Protein ◽  
Underlying Mechanism ◽  
Lipid Transfer ◽  
Β Cells ◽  
Transfer Protein ◽  
Lipid Exchange ◽  
Membrane Tethering

Endoplasmic reticulum (ER) - plasma membrane (PM) contacts are sites of lipid exchange and Ca2+ transport, and both lipid transport proteins and Ca2+ channels specifically accumulate at these locations. In pancreatic β-cells, both lipid- and Ca2+ signaling are essential for insulin secretion. The recently characterized lipid transfer protein TMEM24 dynamically localize to ER-PM contact sites and provide phosphatidylinositol, a precursor of PI(4)P and PI(4,5)P2, to the plasma membrane. β-cells lacking TMEM24 exhibit markedly suppressed glucose-induced Ca2+ oscillations and insulin secretion but the underlying mechanism is not known. We now show that TMEM24 only weakly interact with the PM, and dissociates in response to both diacylglycerol and nanomolar elevations of cytosolic Ca2+. Release of TMEM24 into the bulk ER membrane also enables direct interactions with mitochondria, and we report that loss of TMEM24 results in excessive accumulation of Ca2+ in both the ER and mitochondria and in impaired mitochondria function.

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