WEB FOCUS
Protein transport and trafficking
In this focus
Carrier proteins are used to transport proteins across cellular membranes such as the plasma membrane, endoplasmic reticulum and nuclear envelope. Proteins are also trafficked between membrane-bound organelles inside membrane vesicles. Understanding these two processes has been a major focus of cell biology for several decades. Increasingly the focus is on a molecular description of the structure and mechanism of the complex protein components required to carry out these processes.
This web focus presents a selection of papers covering the latest advances in this area of research. We also present a Review article on protein transport across the endoplasmic reticulum and bacterial plasma membranes. We hope this collection of papers will interest a wide range of biologists engaged in different areas of research.
Image: Courtesy of John Heuser (Washington University) and Thomas Reese (National Institutes of Health)
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Current Research
NEWS AND VIEWS
Cell biology: Pore puzzle
John D. Aitchison & Richard W. Wozniak
Nature 450, 621–622 (29 November 2007) doi:10.1038/450621a
REVIEW
Protein translocation across the eukaryotic ER and bacterial plasma membranes
Tom A. Rapoport
Nature 450, 663–669 (29 November 2007) doi:10.1038/nature06384
ARTICLE
Determining the architectures of macromolecular assemblies
Frank Alber et al.
Nature 450, 683–694 (29 November 2007) doi:10.1038/nature06404
Abstract | Full Text | PDF | Supplementary Information
ARTICLE
The molecular architecture of the nuclear pore complex
Frank Alber et al.
Nature 450, 695–701 (29 November 2007) doi:10.1038/nature06405
Abstract | Full Text | PDF | Supplementary Information
ARTICLE
Shiga toxin induces tubular membrane invaginations for its uptake into cells
Winfried Römer et al.
Nature 450, 670–675 (29 November 2007) doi:10.1038/nature05996
Abstract | Full Text | PDF | Supplementary Information
ARTICLE
A dual–Ca2+-sensor model for neurotransmitter release in a central synapse
Thomas Sudhof
Nature 450, 676–682 (29 November 2007) doi:10.1038/nature06308
Abstract | Full Text | PDF | Supplementary Information
LETTER
How kinesin waits between steps
Teppei Mori, Ronald D. Vale & Michio Tomishige
Nature 450, 750–754 (29 November 2007) doi:10.1038/nature06346
Abstract | Full Text | PDF | Supplementary Information
LETTER
A SNARE-clathrin adaptor interaction reveals a new mode of cargo recognition for clathrin-coated vesicle transport
Sharon E. Miller, Brett M. Collins, Airlie J. McCoy, Margaret S. Robinson & David J. Owen
Nature 450, 570–574 (22 November 2007) doi:10.1038/nature06353
Abstract | Full Text | PDF | Supplementary Information
NEWS AND VIEWS
Microbiology: Pathogen drop-kick
Susanne Pfeffer
Nature 450, 361–362 (15 November 2007) doi:10.1038/450361a
ARTICLE
Legionella pneumophila proteins that regulate Rab1 membrane cycling
Alyssa Ingmundson, Anna Delprato, David G. Lambright & Craig R. Roy
Nature 450, 365–369 (15 November 2007) doi:10.1038/nature06336
Abstract | Full Text | PDF | Supplementary Information
NEWS AND VIEWS
Plant pathology: Deadly special deliveries
Nicholas J. Talbot
Nature 450, 41–43 (1 November 2007) doi:10.1038/450041a
LETTER
A translocation signal for delivery of oomycete effector proteins into host plant cells
Stephen C. Whisson et al.
Nature 450, 115–118 (1 November 2007) doi:10.1038/nature06203
Full Text | PDF | Supplementary Information
LETTER
Functional architecture of the retromer cargo-recognition complex
Aitor Hierro et al.
Nature 449, 1063–1067 (25 October 2007) doi:10.1038/nature06216
Abstract | Full Text | PDF | Supplementary Information
LETTER
Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
Oliver Daumke et al.
Nature 449, 923–927 (18 October 2007) doi:10.1038/nature06173
Abstract | Full Text | PDF | Supplementary Information
LETTER
Structural basis for selective recognition of ESCRT-III by the AAA ATPase Vps4
Takayuki Obita et al.
Nature 449, 735–739 (11 October 2007) doi:10.1038/nature06171
Abstract | Full Text | PDF | Supplementary Information
LETTER
ESCRT-III recognition by VPS4 ATPases
Melissa D. Stuchell-Brereton et al.
Nature 449, 740–744 (11 October 2007) doi:10.1038/nature06172
Abstract | Full Text | PDF | Supplementary Information
LETTER
Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
Martin Beck, Vladan Lui, Friedrich Förster, Wolfgang Baumeister & Ohad Medalia
Nature 449, 611–615 (4 October 2007) doi:10.1038/nature06170
Abstract | Full Text | PDF | Supplementary Information
NEWS AND VIEWS
Cell biology: Taxi service for lipids
Anthony H. Futerman
Nature 449, 35–37 (6 September 2007) doi:10.1038/449035a
ARTICLE
Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide
Giovanni D'Angelo et al.
Nature 449, 62–67 (6 September 2007) doi:10.1038/nature06097
Abstract | Full Text | PDF | Supplementary Information
ANALYSIS
Integrating molecular and network biology to decode endocytosis
Eva M. Schmid & Harvey T. McMahon
Nature 448, 883–888 (23 August 2007) doi:10.1038/nature06031
Full Text | PDF | Supplementary Information
LETTER
Functional diversification of closely related ARF-GEFs in protein secretion and recycling
Sandra Richter et al.
Nature 448, 488–492 (26 July 2007) doi:10.1038/nature05967
Abstract | Full Text | PDF | Supplementary Information
LETTER
An ARF-GEF acting at the Golgi and in selective endocytosis in polarized plant cells
Ooi-kock Teh & Ian Moore
Nature 448, 493–496 (26 July 2007) doi:10.1038/nature06023
Abstract | Full Text | PDF | Supplementary Information
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Podcast
On this week's Nature Podcast, Michael Rout talks about how his team developed a new computational method to describe the architecture of the nuclear
pore complex, the gateway to the nucleus. Click here to listen.
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Video
The gateway to the nucleus is described in detail in a coup for computational biology, published in two papers in
Nature. The new computational method can illustrate the structure of large complexes containing many proteins, and is used to
describe the structure of the nuclear pore complex — the largest protein complex in the cell. The
researchers discuss their results here.
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