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Structural Basis of Vesicle Formation at the Inner Nuclear Membrane

DOI: 10.1016/j.cell.2015.11.029 DOI Help
PMID: 26687357 PMID Help

Authors: Christoph Hagen (University of Oxford) , Kyle C. Dent (Diamond Light Source; , University of Oxford) , Tzviya Zeev-ben-mordehai (University of Oxford) , Michael Grange (University of Oxford) , Jens b. Bosse (Princeton University) , Catheryne Whittle (University of Oxford) , Barbara g. Klupp (Friedrich-Loeffler-Institut) , Alistair Siebert (University of Oxford) , Daven Vasishtan (University of Oxford) , Felix j. B. Bäuerlein (Max Planck Institute of Biochemistry) , Juliana Cheleski Wiggers (University of Oxford) , Stephan Werner (Helmholtz Zentrum Berlin fu¨r Materialien und Energie GmbH) , Peter Guttmann (Helmholtz Zentrum Berlin fu¨r Materialien und Energie GmbH) , Stefan Rehbein (Helmholtz Zentrum Berlin fu¨r Materialien und Energie GmbH) , Katja Henzler (Helmholtz Zentrum Berlin fu¨r Materialien und Energie GmbH) , Justin Demmerle (University of Oxford) , Barbara Adler (Ludwig-Maximilians-Universita¨t Mu¨ nchen) , Ulrich Koszinowski (Ludwig-Maximilians-Universita¨t Mu¨ nchen) , Lothar Schermelleh (University of Oxford) , Gerd Schneider (Helmholtz Zentrum Berlin fu¨r Materialien und Energie GmbH)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cell , VOL 163 , PAGES 1692 - 1701

State: Published (Approved)
Published: December 2015

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials

Facility: ESRF