Functional homologies in vesicle tethering

Autor(en): Kuhlee, Anne
Raunser, Stefan
Ungermann, Christian 
Stichwörter: Biochemistry & Molecular Biology; Biophysics; Cell Biology; CIS-SNARE COMPLEX; CRYSTAL-STRUCTURE; EARLY ENDOSOME; ENDOPLASMIC RETICULUM RETRIEVAL; EXCHANGE FACTOR RABEX-5; HOPS; HOPS COMPLEX; MEMBRANE-FUSION; OLIGOMERIC GOLGI-COMPLEX; Protein complex; STRUCTURAL BASIS; Structural flexibility; Tethering; VACUOLE FUSION; Vesicle
Erscheinungsdatum: 2015
Herausgeber: WILEY
Journal: FEBS LETTERS
Volumen: 589
Ausgabe: 19, A, SI
Startseite: 2487
Seitenende: 2497
Zusammenfassung: 
The HOPS multisubunit tethering factor (MTC) is a macromolecular protein complex composed of six different subunits. It is one of the key components in the perception and subsequent fusion of multivesicular bodies and vacuoles. Electron microscopy studies indicate structural flexibility of the purified HOPS complex. Inducing higher rigidity into HOPS by biochemically modifying the complex declines the potential to mediate SNARE-driven membrane fusion. Thus, we propose that integral flexibility seems to be not only a feature, but of essential need for the function of HOPS. This review focuses on the general features of membrane tethering and fusion. For this purpose, we compare the structure and mode of action of different tethering factors to highlight their common central features and mechanisms. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
ISSN: 00145793
DOI: 10.1016/j.febslet.2015.06.001

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