Molecular mechanisms of calcium-induced membrane fusion

1990 ◽  
Vol 22 (2) ◽  
pp. 157-179 ◽  
Author(s):  
Demetrios Papahadjopoulos ◽  
Shlomo Nir ◽  
Nejat D�zg�nes
Keyword(s):  
Membrane Fusion ◽  
Molecular Mechanisms ◽  
Induced Membrane

scholarly journals SNARE phosphorylation: a control mechanism for insulin-stimulated glucose transport and other regulated exocytic events

2017 ◽  
Vol 45 (6) ◽  
pp. 1271-1277 ◽  
Author(s):  
Kamilla M.E. Laidlaw ◽  
Rachel Livingstone ◽  
Mohammed Al-Tobi ◽  
Nia J. Bryant ◽  
Gwyn W. Gould
Keyword(s):  
Membrane Fusion ◽  
Molecular Mechanisms ◽  
Membrane Receptors ◽  
Multivesicular Bodies ◽  
Attachment Protein ◽  
Protein Receptor ◽  
Sensitive Factor ◽  
Plasma Membrane Receptors ◽  
Regulated Trafficking ◽  
Receptor Family

Trafficking within eukaryotic cells is a complex and highly regulated process; events such as recycling of plasma membrane receptors, formation of multivesicular bodies, regulated release of hormones and delivery of proteins to membranes all require directionality and specificity. The underpinning processes, including cargo selection, membrane fusion, trafficking flow and timing, are controlled by a variety of molecular mechanisms and engage multiple families of lipids and proteins. Here, we will focus on control of trafficking processes via the action of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family of proteins, in particular their regulation by phosphorylation. We will describe how these proteins are controlled in a range of regulated trafficking events, with particular emphasis on the insulin-stimulated delivery of glucose transporters to the surface of adipose and muscle cells. Here, we focus on a few examples of SNARE phosphorylation which exemplify distinct ways in which SNARE machinery phosphorylation may regulate membrane fusion.

scholarly journals A Functional F Analogue of Autographa californica Nucleopolyhedrovirus GP64 from the Agrotis segetum Granulovirus

2008 ◽  
Vol 82 (17) ◽  
pp. 8922-8926 ◽  
Author(s):  
Feifei Yin ◽  
Manli Wang ◽  
Ying Tan ◽  
Fei Deng ◽  
Just M. Vlak ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Plutella Xylostella ◽  
Syncytium Formation ◽  
Low Ph ◽  
Autographa Californica ◽  
Agrotis Segetum ◽  
Induced Membrane ◽  
F Protein ◽  
Autographa Californica Nucleopolyhedrovirus

ABSTRACT The envelope fusion protein F of Plutella xylostella granulovirus is a computational analogue of the GP64 envelope fusion protein of Autographa californica nucleopolyhedrovirus (AcMNPV). Granulovirus (GV) F proteins were thought to be unable to functionally replace GP64 in the AcMNPV pseudotyping system. In the present study the F protein of Agrotis segetum GV (AgseGV) was identified experimentally as the first functional GP64 analogue from GVs. AgseF can rescue virion propagation and infectivity of gp64-null AcMNPV. The AgseF-pseudotyped AcMNPV also induced syncytium formation as a consequence of low-pH-induced membrane fusion.

Insights into a Structure-Based Mechanism of Viral Membrane Fusion

2000 ◽  
Vol 20 (6) ◽  
pp. 557-570 ◽  
Author(s):  
Danika L. LeDuc ◽  
Yeon-Kyun Shin
Keyword(s):  
Membrane Fusion ◽  
General Structure ◽  
Viral Membrane ◽  
Induced Membrane ◽  
Alternative Scenario ◽  
Influenza Hemagglutinin ◽  
Hiv Gp120 ◽  
Viral Membrane Fusion ◽  
Spike Proteins

A number of different viral spike proteins, responsible for membrane fusion, show striking similarities in their core structures. The prospect of developing a general structure-based mechanism seems plausible in light of these newly determined structures. Influenza hemagglutinin (HA) is the best-studied fusion machine, whose action has previously been described by a hypothetical “spring-loaded” model. This model has recently been extended to explain the mechanism of other systems, such as HIV gp120–gp41. However, evidence supporting this idea is insufficient, requiring re-examination of the mechanism of HA-induced membrane fusion. Recent experiments with a shortened construct of HA, which is able to induce lipid mixing, have provided evidence for an alternative scenario for HA-induced membrane fusion and perhaps that of other viral systems.

Host membrane proteins in the HIV-induced membrane fusion: Role in pathogenesis and therapeutic potential of autoantibodies

2021 ◽  
Vol 60 ◽  
pp. 241-248
Author(s):  
Mirna B. Ruiz-Rivera ◽  
Guillermo Gómez-Icazbalceta ◽  
Edmundo Lamoyi ◽  
Leonor Huerta
Keyword(s):  
Membrane Proteins ◽  
Membrane Fusion ◽  
Therapeutic Potential ◽  
Induced Membrane ◽  
Host Membrane

Creating model systems to study molecular mechanisms of C5 convertase-induced Membrane Attack Complex assembly

2017 ◽  
Vol 89 ◽  
pp. 160
Author(s):  
D.J. Doorduijn ◽  
R.D. Gorham ◽  
L. van Bloois ◽  
E. Mastrobattista ◽  
S.H.M. Rooijakkers
Keyword(s):  
Molecular Mechanisms ◽  
Membrane Attack Complex ◽  
Model Systems ◽  
Complex Assembly ◽  
Induced Membrane

Rabies virus-induced membrane fusion

1999 ◽  
Vol 16 (1) ◽  
pp. 21-31 ◽  
Author(s):  
Y Gaudin, ◽  
Christine Tuffereau, ◽  
Peter Durrer, ◽  
Josef Brunner, ◽  
Anne Flamand, ◽  
...  
Keyword(s):  
Membrane Fusion ◽  
Rabies Virus ◽  
Induced Membrane

scholarly journals Antibody-induced membrane fusion in Paramecium

1984 ◽  
Vol 65 (1) ◽  
pp. 153-162
Author(s):  
A. Barnett ◽  
E. Steers
Keyword(s):  
Electron Microscopy ◽  
Membrane Fusion ◽  
Phase Contrast ◽  
Immobilized Cells ◽  
Living Cells ◽  
Immune Serum ◽  
Induced Membrane ◽  
Transmission Electron ◽  
Membrane Changes ◽  
Antigen Antibody

Immobilization of cells by specific immune serum involves crosslinking between immunoglobulin G (IgG) and the i-antigen in the cell membrane. Globular material is seen to accumulate at the ciliary tips by phase-contrast and fluorescence microscopy in a manner analogous to ‘capping’ in more typical eukaryotes. When immobilized cells of Paramecium are examined by scanning electron microscopy, the fused ciliary tips are seen to be distended, discoidal membranes. Transmission electron microscopy often reveals several ciliary axonemes enclosed within a single, enlarged membrane that is oriented with the ferritin-labelled second antibody directed against the i-antigen antibody on the outer surface only. Fixed cells or living cells treated with immune Fab do not show membrane changes, but do bind antibody. Membrane fusion occurs only if cells are alive and the i-antigen is directly or indirectly cross-linked by intact immune IgG.

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