Tuesday, June 30, 2015

Nature Cell Biology contents: July 2015 Volume 17 Number 7, pp 829 - 953

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Nature Cell Biology

TABLE OF CONTENTS

July 2015 Volume 17, Issue 7

Review
Obituary
News and Views
Articles
Corrigenda
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Review

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Proteostasis control by the unfolded protein response   pp829 - 838
Claudio Hetz, Eric Chevet and Scott A. Oakes
doi:10.1038/ncb3184

Obituary

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Alan Hall 1952-2015   pp839 - 840
Filippo G. Giancotti, Cole M. Haynes, Laura M. Machesky, Michael F. Olson and Michael Overholtzer
doi:10.1038/ncb3190

News and Views

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How cells coordinate waste removal through their major proteolytic pathways   pp841 - 842
Sascha Martens and Andreas Bachmair
doi:10.1038/ncb3198
The eukaryotic cell uses two complex machineries to degrade unwanted proteins. The first is the ubiquitin–proteasome system and the second is autophagy. A new study contributes to our understanding of how the two systems interconnect to coordinate protein degradation.

See also: Article by Cha-Molstad et al.

Rubicon swaps autophagy for LAP   pp843 - 845
Keith B. Boyle and Felix Randow
doi:10.1038/ncb3197
Phagocytic cells engulf their prey into vesicular structures called phagosomes, of which a certain proportion becomes demarcated for enhanced maturation by a process called LC3-associated phagocytosis (LAP). Light has now been shed on the molecular requirements of LAP, establishing a central role for the protein Rubicon in the immune response to Aspergillus fumigatus.

See also: Article by Martinez et al.

Super-resolution links vinculin localization to function in focal adhesions   pp845 - 847
Grégory Giannone
doi:10.1038/ncb3196
Integrin-based focal adhesions integrate biochemical and biomechanical signals from the extracellular matrix and the actin cytoskeleton. The combination of three-dimensional super-resolution imaging and loss- or gain-of-function protein mutants now links the nanoscale dynamic localization of proteins to their activation and function within focal adhesions.

See also: Article by Case et al.

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Articles

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Pulsatile cell-autonomous contractility drives compaction in the mouse embryo   pp849 - 855
Jean-Léon Maître, Ritsuya Niwayama, Hervé Turlier, François Nédélec and Takashi Hiiragi
doi:10.1038/ncb3185
By measuring surface tensions in developing mouse embryos, Maître and colleagues show that compaction of the blastomere stage embryo is driven by downregulation of actomyosin at cell–cell contacts.

The oncogene c-Jun impedes somatic cell reprogramming   pp856 - 867
Jing Liu, Qingkai Han, Tianran Peng, Meixiu Peng, Bei Wei et al.
doi:10.1038/ncb3193
Pei and colleagues report that the oncogene c-Jun acts as a somatic cell reprogramming barrier, and that its truncated dominant-negative form can substitute for Oct4 in reprogramming.

The kinetochore encodes a mechanical switch to disrupt spindle assembly checkpoint signalling   pp868 - 879
Pavithra Aravamudhan, Alan A. Goldfarb and Ajit P. Joglekar
doi:10.1038/ncb3179
Joglekar and colleagues show that in budding yeast, kinetochore–microtubule attachment mediates silencing of the spindle assembly checkpoint through physical separation of Mps1 kinase from its substrate Spc105.

Molecular mechanism of vinculin activation and nanoscale spatial organization in focal adhesions   pp880 - 892
Lindsay B. Case, Michelle A. Baird, Gleb Shtengel, Sharon L. Campbell, Harald F. Hess et al.
doi:10.1038/ncb3180
Waterman and colleagues use super-resolution microscopy and biosensor technology to characterize the spatiotemporal regulation of the protein interactions within focal adhesions that control vinculin activation and function during focal adhesion maturation.

See also: News and Views by Giannone

Molecular characterization of LC3-associated phagocytosis reveals distinct roles for Rubicon, NOX2 and autophagy proteins   pp893 - 906
Jennifer Martinez, R. K. Subbarao Malireddi, Qun Lu, Larissa Dias Cunha, Stephane Pelletier et al.
doi:10.1038/ncb3192
Green and colleagues characterize LC3-associated phagocytosis as a process that depends on Rubicon, Beclin-1, UVRAG and VPS34 but not on canonical autophagy proteins.

See also: News and Views by Boyle & Randow

Microtubule-associated proteins control the kinetics of microtubule nucleation   pp907 - 916
Michal Wieczorek, Susanne Bechstedt, Sami Chaaban and Gary J. Brouhard
doi:10.1038/ncb3188
Through single-molecule analyses, Brouhard and colleagues find a kinetic barrier to microtubule nucleation, which can be overcome by the action of the microtubule-associated proteins XMAP215 and TPX2.

Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding   pp917 - 929
Hyunjoo Cha-Molstad, Ki Sa Sung, Joonsung Hwang, Kyoung A. Kim, Ji Eun Yu et al.
doi:10.1038/ncb3177
Kim and colleagues and Kwon and colleagues reveal that amino-terminal arginylation of BiP promotes its targeting to autophagy adaptor p62 and subsequent lysosomal degradation of BiP, p62 and associated cargo.

See also: News and Views by Martens & Bachmair

A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation regulates autophagy   pp930 - 942
Guowu Hu, Travis McQuiston, Amélie Bernard, Yoon-Dong Park, Jin Qiu et al.
doi:10.1038/ncb3189
Williamson and colleagues demonstrate that mRNA-decapping enzyme Dcp2 is phosphorylated by mTORC1, leading to degradation of Atg mRNA and suppression of autophagy, influencing immunity and inflammation.

Mechanosensitive pannexin-1 channels mediate microvascular metastatic cell survival   pp943 - 952
Paul W. Furlow, Steven Zhang, T. David Soong, Nils Halberg, Hani Goodarzi et al.
doi:10.1038/ncb3194
Tavazoie and colleagues report that activation of pannexin-1 channels and the subsequent stimulation of autocrine purinergic signalling promotes the survival of disseminated cancer cells in the microvasculature of metastasis target organs.

Corrigenda

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Corrigenda: Kinetochore components are required for central spindle assembly   p953
Gilliane Maton, Frances Edwards, Benjamin Lacroix, Marine Stefanutti, Kimberley Laband et al.
doi:10.1038/ncb3199

Corrigenda: MCUR1 is an essential component of mitochondrial Ca2+ uptake that regulates cellular metabolism   p953
Karthik Mallilankaraman, César Cárdenas, Patrick J. Doonan, Harish C. Chandramoorthy, Krishna M. Irrinki et al.
doi:10.1038/ncb3202

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