Structural Basis of Vesicle Formation at the Inner Nuclear Membrane.

TitleStructural Basis of Vesicle Formation at the Inner Nuclear Membrane.
Publication TypeJournal Article
Year of Publication2015
AuthorsHagen, C, Dent, KC, Zeev-Ben-Mordehai, T, Grange, M, Bosse, JB, Whittle, C, Klupp, BG, C Siebert, A, Vasishtan, D, Bäuerlein, FJB, Cheleski, J, Werner, S, Guttmann, P, Rehbein, S, Henzler, K, Demmerle, J, Adler, B, Koszinowski, U, Schermelleh, L, Schneider, G, Enquist, LW, Plitzko, JM, Mettenleiter, TC, Grünewald, K
JournalCell
Volume163
Issue7
Pagination1692-701
Date Published2015 Dec 17
ISSN1097-4172
KeywordsActive Transport, Cell Nucleus, Animals, Capsid, Cercopithecus aethiops, Cryoelectron Microscopy, Electron Microscope Tomography, Herpesvirus 1, Human, Herpesvirus 1, Suid, Nuclear Envelope, Nuclear Proteins, Pyrimidine Dimers, Scattering, Small Angle, Transport Vesicles, Vero Cells, Viral Proteins
Abstract

<p>Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane. To understand the structural underpinning for this trafficking, we investigated nuclear egress of progeny herpesvirus capsids where capsid envelopment is mediated by two viral proteins, forming the nuclear egress complex (NEC). Using a multi-modal imaging approach, we visualized the NEC in situ forming coated vesicles of defined size. Cellular electron cryo-tomography revealed a protein layer showing two distinct hexagonal lattices at its membrane-proximal and membrane-distant faces, respectively. NEC coat architecture was determined by combining this information with integrative modeling using small-angle X-ray scattering data. The molecular arrangement of the NEC establishes the basic mechanism for budding and scission of tailored vesicles at the INM.</p>

DOI10.1016/j.cell.2015.11.029
Alternate JournalCell
PubMed ID26687357
PubMed Central IDPMC4701712
Grant List060208/Z/00/Z / / Wellcome Trust / United Kingdom
090532/Z/09/Z / / Wellcome Trust / United Kingdom
090895/Z/09/Z / / Wellcome Trust / United Kingdom
093305/Z/10/Z / / Wellcome Trust / United Kingdom