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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Structural Basis of Vesicle Formation at the Inner Nuclear Membrane

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Author(s):
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Hagen, Christoph [1] ; Dent, Kyle C. [2, 1] ; Zeev-Ben-Mordehai, Tzviya [1] ; Grange, Michael [1] ; Bosse, Jens B. [3] ; Whittle, Cathy [1] ; Klupp, Barbara G. [4] ; Siebert, C. Alistair [1] ; Vasishtan, Daven [1] ; Baeuerlein, Felix J. B. [5] ; Cheleski, Juliana [1] ; Werner, Stephan [6] ; Guttmann, Peter [6] ; Rehbein, Stefan [6] ; Henzler, Katja [6] ; Demmerle, Justin [7] ; Adler, Barbara [8] ; Koszinowski, Ulrich [8] ; Schermelleh, Lothar [7] ; Schneider, Gerd [6] ; Enquist, Lynn W. [3] ; Plitzko, Juergen M. [5] ; Mettenleiter, Thomas C. [4] ; Gruenewald, Kay [1]
Total Authors: 24
Affiliation:
[1] Univ Oxford, Wellcome Trust Ctr Human Genet, Oxford Particle Imaging Ctr, Div Struct Biol, Oxford OX3 7BN - England
[2] Diamond Light Source Ltd, Didcot OX11 0DE, Oxon - England
[3] Princeton Univ, Princeton Neurosci Inst, Dept Mol Biol, Princeton, NJ 08544 - USA
[4] Friedrich Loeffler Inst, Inst Mol Virol & Cell Biol, D-17493 Greifswald - Germany
[5] Max Planck Inst Biochem, Dept Mol Struct Biol, D-82152 Martinsried - Germany
[6] Helmholtz Zentrum Berlin Mat & Energie GmbH, D-12489 Berlin - Germany
[7] Univ Oxford, Dept Biochem, Micron Oxford, Oxford OX1 3QU - England
[8] Univ Munich, Max Von Pettenkofer Inst, D-80336 Munich - Germany
Total Affiliations: 8
Document type: Journal article
Source: Cell; v. 163, n. 7, p. 1692-1701, DEC 17 2015.
Web of Science Citations: 68
Abstract

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. (AU)

FAPESP's process: 13/24972-1 - Cryo-electron tomography to visualize macromolecular organization
Grantee:Juliana Cheleski Wiggers
Support Opportunities: Scholarships abroad - Research Internship - Post-doctor