scholarly journals Folded Monomers and Hexamers of the Ectodomain of the HIV gp41 Membrane Fusion Protein: Potential Roles in Fusion and Synergy Between the Fusion Peptide, Hairpin, and Membrane-Proximal External Region

Biochemistry ◽  
2014 ◽  
Vol 53 (46) ◽  
pp. 7184-7198 ◽  
Author(s):  
Koyeli Banerjee ◽  
David P. Weliky
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Fusion Peptide ◽  
External Region ◽  
Membrane Proximal External Region ◽  
Membrane Fusion Protein ◽  
Hiv Gp41

scholarly journals Structural and Functional Properties of an Unusual Internal Fusion Peptide in a Nonenveloped Virus Membrane Fusion Protein

2004 ◽  
Vol 78 (6) ◽  
pp. 2808-2818 ◽  
Author(s):  
Maya Shmulevitz ◽  
Raquel F. Epand ◽  
Richard M. Epand ◽  
Roy Duncan
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Fusion Proteins ◽  
Fusion Peptide ◽  
Loop Structure ◽  
Fusion Peptides ◽  
Enveloped Virus ◽  
Membrane Fusion Protein ◽  
Virus Fusion ◽  
Nonenveloped Virus

ABSTRACT The avian and Nelson Bay reoviruses are two of only a limited number of nonenveloped viruses capable of inducing cell-cell membrane fusion. These viruses encode the smallest known membrane fusion proteins (p10). We now show that a region of moderate hydrophobicity we call the hydrophobic patch (HP), present in the small N-terminal ectodomain of p10, shares the following characteristics with the fusion peptides of enveloped virus fusion proteins: (i) an abundance of glycine and alanine residues, (ii) a potential amphipathic secondary structure, (iii) membrane-seeking characteristics that correspond to the degree of hydrophobicity, and (iv) the ability to induce lipid mixing in a liposome fusion assay. The p10 HP is therefore predicted to provide a function in the mechanism of membrane fusion similar to those of the fusion peptides of enveloped virus fusion peptides, namely, association with and destabilization of opposing lipid bilayers. Mutational and biophysical analysis suggested that the internal fusion peptide of p10 lacks alpha-helical content and exists as a disulfide-stabilized loop structure. Similar kinked structures have been reported in the fusion peptides of several enveloped virus fusion proteins. The preservation of a predicted loop structure in the fusion peptide of this unusual nonenveloped virus membrane fusion protein supports an imperative role for a kinked fusion peptide motif in biological membrane fusion.

scholarly journals A membrane fusion protein, Ykt6, regulates epithelial cell migration via microRNA-mediated suppression of Junctional Adhesion Molecule A

Cell Cycle ◽  
2018 ◽  
Vol 17 (14) ◽  
pp. 1812-1831 ◽  
Author(s):  
Nayden G. Naydenov ◽  
Supriya Joshi ◽  
Alex Feygin ◽  
Siddharth Saini ◽  
Larisa Litovchick ◽  
...  
Keyword(s):  
Cell Migration ◽  
Epithelial Cell ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Adhesion Molecule ◽  
Membrane Fusion Protein ◽  
Epithelial Cell Migration
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