TABLE OF CONTENTS
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June 2016 Volume 23, Issue 6 |
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Focus | Top |
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 | | Focus on Membrane Proteins |  | Focus issue: June 2016 Volume 23 No 6 | |
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Editorial | Top |
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Focus on Membrane Proteins Cellular gatekeepers p463 doi:10.1038/nsmb.3246 In a common yet effective analogy, a cell can be compared to a fortified city, in which lipid membranes form the defensive walls, and membrane proteins function as gates and checkpoints that control the transit of molecules and information across these walls. We evoke this concept on the cover of this special Focus on Membrane Proteins. |
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Commentary | Top |
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Focus on Membrane Proteins Atomic-level analysis of membrane-protein structure pp464 - 467 Wayne A Hendrickson doi:10.1038/nsmb.3215 Wayne Hendrickson discusses the consortium efforts and developments in methodology that in recent years have allowed unprecedented advances in atomic-structure determination of membrane proteins. |
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Perspectives | Top |
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Focus on Membrane Proteins NMR as a tool to investigate the structure, dynamics and function of membrane proteins pp468 - 474 Binyong Liang and Lukas K Tamm doi:10.1038/nsmb.3226 This Perspective provides an overview of recent progress, successes, challenges and future opportunities in the application of solution NMR and solid-state NMR methods to study the structure, dynamics and function of membrane proteins. |
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Focus on Membrane Proteins Toward high-resolution computational design of the structure and function of helical membrane proteins pp475 - 480 Patrick Barth and Alessandro Senes doi:10.1038/nsmb.3231 This Perspective provides an overview of the major advances in recent years in the computational design and structure prediction of α-helical membrane proteins. |
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Focus on Membrane Proteins Nanodiscs for structural and functional studies of membrane proteins pp481 - 486 Ilia G Denisov and Stephen G Sligar doi:10.1038/nsmb.3195 The use of nanodiscs is substantially fostering structural and functional studies of membrane protein. This Perspective summarizes the recent use of nanodiscs as an invaluable tool for the characterization of membrane proteins. |
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Reviews | Top |
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Focus on Membrane Proteins Mechanistic diversity in ATP-binding cassette (ABC) transporters pp487 - 493 Kaspar P Locher doi:10.1038/nsmb.3216 ABC transporters use ATP hydrolysis to translocate substrates across cell membranes. Kaspar Locher reviews the mechanistic diversity of ABC transporters, as has emerged from recent structural studies, and discusses future directions for investigation of ABC-transporter-catalyzed reactions. |
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Focus on Membrane Proteins Structural mechanisms of activation and desensitization in neurotransmitter-gated ion channels pp494 - 502 Andrew J R Plested doi:10.1038/nsmb.3214 Numerous recent crystal and cryo-EM structures have greatly advanced understanding of the functional mechanisms of neurotransmitter-gated ion channels. This Review discusses the structural basis of activation and desensitization mechanisms in glutamate and cysteine-loop receptors. |
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Obituary | Top |
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Knud Hermann Nierhaus 1941-2016 pp503 - 504 Daniel N Wilson and Christian M T Spahn doi:10.1038/nsmb.3239 |
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News and Views | Top |
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Articles | Top |
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Crystal structure of the prefusion surface glycoprotein of the prototypic arenavirus LCMV pp513 - 521 Kathryn M Hastie, Sebastien Igonet, Brian M Sullivan, Pierre Legrand, Michelle A Zandonatti et al. doi:10.1038/nsmb.3210 The crystal structure of the GP1-GP2 complex of the prototypical arenavirus LCMV in prefusion form sheds light on the conformational changes that the arenavirus glycoprotein undergoes to cause fusion. |
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Long noncoding RNA LINP1 regulates repair of DNA double-strand breaks in triple-negative breast cancer pp522 - 530 Youyou Zhang, Qun He, Zhongyi Hu, Yi Feng, Lingling Fan et al. doi:10.1038/nsmb.3211 New data reveal that LINP1, a lncRNA overexpressed in triple-negative breast cancer, interacts with the Ku70-Ku80 complex and DNA-PKcs, thereby promoting NHEJ-mediated DNA double-strand-break repair.
See also: News and Views by Lees-Miller et al. |
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Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery pp531 - 539 Alexis Huet, Alexander M Makhov, Jamie B Huffman, Matthijn Vos, Fred L Homa et al. doi:10.1038/nsmb.3212 Capsids from two herpesviruses (HSV-1 and PRV), imaged inside intact virions, are analyzed by cryo-EM. The maps allowed the construction of a complete model of subunit and domain organization, revealing extensive subunit contacts. |
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BRD4 is a histone acetyltransferase that evicts nucleosomes from chromatin pp540 - 548 Ballachanda N Devaiah, Chanelle Case-Borden, Anne Gegonne, Chih Hao Hsu, Qingrong Chen et al. doi:10.1038/nsmb.3228 In vitro and in vivo analyses show that BRD4 has intrinsic acetyltransferase activity targeting histones H3 and H4, and BRD4 acetylation of H3 K122 results in histone eviction, nucleosome clearance and chromatin decompaction. |
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Structure of a group II intron in complex with its reverse transcriptase pp549 - 557 Guosheng Qu, Prem Singh Kaushal, Jia Wang, Hideki Shigematsu, Carol Lyn Piazza et al. doi:10.1038/nsmb.3220 A 3.8-A cryo-EM structure of a bacterial group IIA intron in complex with its intron-encoded protein reveals how the reverse transcriptase domain interacts with the mobile intron RNA as well as structural similarities with eukaryotic telomerase and spliceosomal components.
See also: News and Views by Piccirilli & Staley | Article by Zhao & Pyle |
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Crystal structures of a group II intron maturase reveal a missing link in spliceosome evolution pp558 - 565 Chen Zhao and Anna Marie Pyle doi:10.1038/nsmb.3224 Crystal structures of the reverse transcriptase domains of two group II intron-encoded proteins reveal their similarity to the RT domain of splicing factor Prp8, thus suggesting a common ancestry shared by group II introns and the spliceosome.
See also: News and Views by Piccirilli & Staley | Article by Qu et al. |
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Lactase nonpersistence is directed by DNA-variation-dependent epigenetic aging pp566 - 573 Viviane Labrie, Orion J Buske, Edward Oh, Richie Jeremian, Carolyn Ptak et al. doi:10.1038/nsmb.3227 Age-dependent epigenetic changes that are influenced by genetic factors contribute to lactase nonpersistence, which is linked to the inability of adult mammals to digest lactose.
See also: News and Views by Swallow & Troelsen |
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Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation pp574 - 579 Eugene Valkov, Sowndarya Muthukumar, Chung-Te Chang, Stefanie Jonas, Oliver Weichenrieder et al. doi:10.1038/nsmb.3232 Crystal structures, along with biochemistry data, capture the active form of the Dcp2 decapping enzyme in complex with Dcp1 and a peptide from Edc1, thus revealing the mechanism of activation by Dcp1 and Edc1 activators. |
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Functional interplay between MSL1 and CDK7 controls RNA polymerase II Ser5 phosphorylation pp580 - 589 Sarantis Chlamydas, Herbert Holz, Maria Samata, Tomasz Chelmicki, Plamen Georgiev et al. doi:10.1038/nsmb.3233 MSL1, a component of the Drosophila dosage compensation complex, genetically and biochemically interacts with CDK7, a subunit of the TFIIH transcription factor, thus revealing a complex interplay between MSL1 and the general transcriptional machinery. |
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Mechanism of extracellular ion exchange and binding-site occlusion in a sodium/calcium exchanger pp590 - 599 Jun Liao, Fabrizio Marinelli, Changkeun Lee, Yihe Huang, Jose D Faraldo-Gomez et al. doi:10.1038/nsmb.3230 A series of crystal structures and calculated free-energy landscapes of a Na+/Ca2+ exchanger explain how its alternating-access mechanism is controlled by the ion occupancy, thus leading to coupled antiport. |
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Allosteric inhibition of antiapoptotic MCL-1 pp600 - 607 Susan Lee, Thomas E Wales, Silvia Escudero, Daniel T Cohen, James Luccarelli et al. doi:10.1038/nsmb.3223 Identification of an allosteric mechanism disrupting the antiapoptotic BH3 binding activity of MCL-1 offers a new approach for targeting the apoptotic resistance of human cancers.
See also: News and Views by Konermann |
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Resource | Top |
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Multilayered proteomics reveals molecular switches dictating ligand-dependent EGFR trafficking pp608 - 618 Chiara Francavilla, Moreno Papetti, Kristoffer T G Rigbolt, Anna-Kathrine Pedersen, Jon O Sigurdsson et al. doi:10.1038/nsmb.3218 Analysis of changes in the EGFR interactome, ubiquitinome, phosphoproteome and proteome in response to EGF or TGF-α identifies RAB7 phosphorylation and RCP recruitment to EGFR as ligand-specific switches controlling receptor trafficking, signal duration and cellular responses. |
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