Although membrane fusion plays key roles in intracellular trafficking, neurotransmitter release, and viral infection, its underlying molecular mechanism and its energy landscape are not well understood.
Ca2+-triggered membrane fusion is the key element of regulated exocytosis [1], [2].
DOI: http://dx.doi.org/10.7554/eLife.00109.002 There are many examples where protein-mediated membrane fusion plays a key role, such as entry of enveloped viruses, fertilization, development, carcinogenesis, intracellular trafficking, secretion, and neurotransmitter release (Rothman, 1994; Jahn et al., 2003; Jahn and Scheller, 2006; Harrison, 2008; Rizo and Rosenmund, 2008; Moreau et al., 2011).
Questions such as these cannot be addressed by qualitative speculations, but their answers will likely provide important mechanistic insights into the basis of biologically catalyzed membrane fusion, an evolutionarily innovation key to the emergence of eukaryotic life.
The haemagglutinin (HA) envelope glycoprotein mediates influenza virus membrane fusion and hence has a key function in host cell invasion by this major human pathogen.
A key element of membrane fusion reactions in biology is the involvement of specific fusion proteins.
The membrane-proximal external region (MPER) is a highly conserved region of the envelope glycoprotein (Env) gp41 subunit near the viral envelope surface, and it plays a key role in membrane fusion.
αSNAP is a ubiquitous protein that plays a key role in membrane fusion and exocytosis.
Soluble N-ethylmaleimide sensitive factor attachment protein α (αSNAP) is a ubiquitous protein present in all eukaryotic cells playing a key role in membrane fusion [1].
Thus, while the natural antibody response blocks cell binding [27], it evidently fails to inactivate the key process of membrane fusion.
