The role of transmembrane domains in membrane fusion

Autor(en): Langosch, D.
Hofmann, M.
Ungermann, C. 
Stichwörter: Biochemistry & Molecular Biology; Cell Biology; CONFORMATIONAL-CHANGE; CONSERVED GLYCINE RESIDUES; fusion pore; hemifusion; HEMIFUSION INTERMEDIATE; IMMUNODEFICIENCY-VIRUS TYPE-1; membrane fusion; PROTEIN INTERACTIONS; SECONDARY STRUCTURE; SNARE; SNARE COMPLEX; SPANNING DOMAIN; transmembrane domain; VACUOLE FUSION; VIRAL FUSION
Erscheinungsdatum: 2007
Herausgeber: SPRINGER BASEL AG
Journal: CELLULAR AND MOLECULAR LIFE SCIENCES
Volumen: 64
Ausgabe: 7-8
Startseite: 850
Seitenende: 864
Zusammenfassung: 
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 features. Their transmembrane domains are now known to be critical for the fusion reaction. We discuss at which stages they might contribute to bilayer mixing.
ISSN: 1420682X
DOI: 10.1007/s00018-007-6439-x

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