The role of transmembrane domains in membrane fusion

  title={The role of transmembrane domains in membrane fusion},
  author={Dieter Langosch and Mathias W Hofmann and Christian Ungermann},
  journal={Cellular and Molecular Life Sciences},
Abstract.Biological membrane fusion is driven by different types of molecular fusion machines. Most of these proteins are membrane-anchored by single transmembrane domains. SNARE proteins are essential for intracellular membrane fusion along the secretory and endocytic pathway, while various viral fusogens mediate infection of eukaryotic cells by enveloped viruses. Although both types of fusion proteins are evolutionarily quite distant from each other, they do share a number of structural and… 

Functional relevance of transmembrane domains in membrane fusion

This work describes these proteins as being instrumental in viral, intracellular and developmental fusion, and focuses on the structure and dynamics of the transmembrane segment that anchors the fusion proteins to the bilayer, and its role in driving fusion.

Viral Membrane Fusion and the Transmembrane Domain

This work summarizes developments made in the past decade that have contributed to the understanding of the transmembrane region of viral fusion proteins, highlighting not only their critical role in the membrane fusion process, but further demonstrating their involvement in several aspects of the viral lifecycle.

Models of Membrane Fusion

An overview of common fusion types, current knowledge of corresponding fusion mechanisms, and efforts to model membrane fusion is given, which includes both phenomenological modeling and computer simulations.

Mechanics of membrane fusion

The conserved fusion-through-hemifusion pathway of merger between biological membranes is discussed and it is proposed that the entire progression, from the close juxtaposition of membrane bilayers to the expansion of a fusion pore, is controlled by protein-generated membrane stresses.

Transmembrane-domain determinants for SNARE-mediated membrane fusion

Structural length requirements, largely confined to the C-terminal half of the VAMP2 TMD, seem to be essential for SNARE-mediated membrane-fusion events in cells.

Role of the transmembrane domain in SNARE protein mediated membrane fusion: peptide nucleic acid/peptide model systems.

Peptide nucleic acids (PNAs) are used as excellent candidates for mimicking the SNARE recognition motif by forming well-characterized duplex structures and a series of PNA/peptide hybrids differing in the length of TMDs and charges at the C-terminal end is presented.

The Multifaceted Role of SNARE Proteins in Membrane Fusion

This review summarizes current knowledge on the intricate molecular mechanisms underlying exocytosis triggered and catalyzed by SNARE proteins and particular attention is given to the function of the peptidic SNARE membrane anchors and the role of SNARE-lipid interactions in fusion.

Structural Determinants for the Membrane Insertion of the Transmembrane Peptide of Hemagglutinin from Influenza Virus

From the results, it could be concluded that three independent TM peptide segments arrange themselves in a parallel arrangement, very similarly to what is observed for the C-terminal regions of the hemagglutinin crystallographic structure of the protein, to where the segments are attached.

Structural features of fusogenic model transmembrane domains that differentially regulate inner and outer leaflet mixing in membrane fusion

This work investigates the impact of different structural features of LV-peptide TMDs on inner and outer leaflet mixing and finds that fusion driven by the helical peptides involves a hemifusion intermediate as previously seen for natural fusion proteins.



Intracellular and viral membrane fusion: a uniting mechanism.

Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

It is found that, to a marked degree, the pattern of membrane flow in the cell is encoded and recapitulated by its isolated SNARE proteins, as predicted by the SNARE hypothesis.

Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity.

It is shown that the presence of synthetic peptides representing the transmembrane segments of the presynaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) synaptobrevin II or syntaxin 1A in liposomal membranes drives their fusion.

The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion.

The results imply a direct role for the residues in the membrane-spanning domain of the murine leukemia virus envelope protein in membrane fusion and its regulation and support the thesis that membrane- spanning domains possess a sequence-dependent function in other protein-mediated membrane fusion events.

Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing

Structural studies are revealing the mechanisms by which SNARES form complexes and interact with other proteins and it is now apparent that the SNARE transmembrane segment not only anchors the protein but engages in SNARE-SNARE interactions and plays an active role in fusion.

Protein-lipid interplay in fusion and fission of biological membranes.

The phenomenology and the pathways of the well-characterized reactions of biological remodeling, such as fusion mediated by influenza hemagglutinin, are compared with those studied for protein-free bilayers and some proteins involved in fusion and fission are considered.