Table of contents
November 2006, Volume 8 No 11 pp1179-1309
About the coverFocus
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This issue features a joint Focus — Systems biology: a user's guide — between Nature Cell Biology and Nature Reviews Molecular Cell Biology. The full Focus content can be found online, together with a library featuring articles on systems biology from our past issues and from other Nature Publishing Group journals. Print subscribers will receive a reprint supplement containing the entire Focus content. |
Editorial
All systems go! - p1179
doi:10.1038/ncb1106-1179
Full Text - All systems go! | PDF (102 KB) - All systems go!
Reviews
Focus on Systems biology: a user's guide
Linking publication, gene and protein data - pp1183 - 1189
Paul Kersey & Rolf Apweiler
doi:10.1038/ncb1495
Abstract - | Full Text - Linking publication, gene and protein data | PDF (773 KB) - Linking publication, gene and protein data | Supplementary information
Focus on Systems biology: a user's guide
Modelling data across labs, genomes, space and time - pp1190 - 1194
Jason R. Swedlow, Suzanna E. Lewis & Ilya G. Goldberg
doi:10.1038/ncb1496
Abstract - | Full Text - Modelling data across labs, genomes, space and time | PDF (183 KB) - Modelling data across labs, genomes, space and time
Focus on Systems biology: a user's guide
Physicochemical modelling of cell signalling pathways - pp1195 - 1203
Bree B. Aldridge, John M. Burke, Douglas A. Lauffenburger & Peter K. Sorger
doi:10.1038/ncb1497
Abstract - | Full Text - Physicochemical modelling of cell signalling pathways | PDF (565 KB) - Physicochemical modelling of cell signalling pathways
Focus on Systems biology: a user's guide
Modelling microtubule patterns - pp1204 - 1211
Eric Karsenti, François Nédélec & Thomas Surrey
doi:10.1038/ncb1498
Abstract - | Full Text - Modelling microtubule patterns | PDF (351 KB) - Modelling microtubule patterns
Book Review
Biofluorescence: the making of a new technology - p1212
Jennifer Lippincott-Schwartz reviews Aglow in the dark: The revolutionary science of biofluorescence by Vincent Pieribone & David Gruber
doi:10.1038/ncb1106-1212
Full Text - Biofluorescence: the making of a new technology | PDF (117 KB) - Biofluorescence: the making of a new technology
News and Views
ROS as a tumour suppressor? - pp1213 - 1215
Matthew R. Ramsey & Norman E. Sharpless
doi:10.1038/ncb1106-1213
Senescence is an important mechanism for suppressing mammalian tumours and it may also contribute to aging. A new study suggests that changes in the metabolism of oxygen radicals are important for establishing senescence and blocking cytokinesis to ensure senescent cells never divide again.
Full Text - ROS as a tumour suppressor? | PDF (153 KB) - ROS as a tumour suppressor?
Ahead of the curve: mitochondrial fusion and phospholipase D - pp1215 - 1217
Robert E. Jensen & Hiromi Sesaki
doi:10.1038/ncb1106-1215
A new study has identified a novel phospholipase D (PLD) that is located in the mitochondrial outer membrane and is required for organelle fusion. As PLD-catalysed production of fusogenic lipids is critical for many examples of membrane fusion (such as those mediated by SNAREs), this startling finding raises the possibility that mitochondria use a mechanism common to other cellular fusion events.
Full Text - Ahead of the curve: mitochondrial fusion and phospholipase D | PDF (212 KB) - Ahead of the curve: mitochondrial fusion and phospholipase D
PERing in their sleep - p1217
Sowmya Swaminathan
doi:10.1038/ncb1106-1217
Full Text - PERing in their sleep | PDF (221 KB) - PERing in their sleep
Working out coupled monoubiquitination - pp1218 - 1219
Kaisa Haglund & Harald Stenmark
doi:10.1038/ncb1106-1218
Ubiquitin receptors that bind ubiquitinated proteins through ubiquitin-binding domains have key roles in various cellular processes. These receptors are often themselves monoubiquitinated, referred to as coupled monoubiquitination. Now, coupled monoubiquitination has been shown to involve monoubiquitination of a ubiquitin ligase and its subsequent interaction with a ubiquitin receptor.
Full Text - Working out coupled monoubiquitination | PDF (143 KB) - Working out coupled monoubiquitination
SePARating polarity and proliferation in ErbB2 oncogenesis - pp1220 - 1222
Stephanie J. Walker & Joan S. Brugge
doi:10.1038/ncb1106-1220
Loss of tissue organization, including disruption of epithelial polarity, is a feature of many carcinomas. Activation of the oncogenic receptor tyrosine kinase, ErbB2, induces alterations in epithelial architecture, but the mechanisms underlying this effect are poorly understood. New data suggests that the polarity proteins, Par6 and atypical PKC, may affect epithelial polarity and cell survival through interactions with an ErbB2 receptor complex.
Full Text - SePARating polarity and proliferation in ErbB2 oncogenesis | PDF (516 KB) - SePARating polarity and proliferation in ErbB2 oncogenesis
Articles
VEGF controls endothelial-cell permeability by promoting the
-arrestin-dependent endocytosis of VE-cadherin - pp1223 - 1234
Julie Gavard & J. Silvio Gutkind
doi:10.1038/ncb1486
Abstract - | Full Text - VEGF controls endothelial-cell permeability by promoting the
-arrestin-dependent endocytosis of VE-cadherin | PDF (2,404 KB) - VEGF controls endothelial-cell permeability by promoting the
-arrestin-dependent endocytosis of VE-cadherin | Supplementary information
Par6–aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control - pp1235 - 1245
Victoria Aranda, Teresa Haire, Marissa E. Nolan, Joseph P. Calarco, Avi Z. Rosenberg, James P. Fawcett, Tony Pawson & Senthil K. Muthuswamy
doi:10.1038/ncb1485
Abstract - | Full Text - Par6–aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control | PDF (1,862 KB) - Par6–aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control | Supplementary information
See also: News and Views by Walker & Brugge
Molecular mechanisms of coupled monoubiquitination - pp1246 - 1254
Tanja Woelk, Barbara Oldrini, Elena Maspero, Stefano Confalonieri, Elena Cavallaro, Pier Paolo Di Fiore & Simona Polo
doi:10.1038/ncb1484
First Paragraph - | Full Text - Molecular mechanisms of coupled monoubiquitination | PDF (3,703 KB) - Molecular mechanisms of coupled monoubiquitination | Supplementary information
See also: News and Views by Haglund & Stenmark
Letters
A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis - pp1255 - 1262
Seok-Yong Choi, Ping Huang, Gary M. Jenkins, David C. Chan, Juergen Schiller & Michael A. Frohman
doi:10.1038/ncb1487
First Paragraph - | Full Text - A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis | PDF (2,388 KB) - A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis | Supplementary information
See also: News and Views by Jensen & Sesaki
TRAPPII subunits are required for the specificity switch of a Ypt–Rab GEF - pp1263 - 1269
Nadya Morozova, Yongheng Liang, Andrei A. Tokarev, Shu H. Chen, Randal Cox, Jelena Andrejic, Zhanna Lipatova, Vicki A. Sciorra, Scott D. Emr & Nava Segev
doi:10.1038/ncb1489
First Paragraph - | Full Text - TRAPPII subunits are required for the specificity switch of a Ypt–Rab GEF | PDF (4,880 KB) - TRAPPII subunits are required for the specificity switch of a Ypt–Rab GEF | Supplementary information
CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse - pp1270 - 1276
Regina Tavano, Rita Lucia Contento, Sonia Jimenez Baranda, Marzia Soligo, Loretta Tuosto, Santos Manes & Antonella Viola
doi:10.1038/ncb1492
First Paragraph - | Full Text - CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse | PDF (1,264 KB) - CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse | Supplementary information
CUL4–DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation - pp1277 - 1283
Leigh Ann Higa, Min Wu, Tao Ye, Ryuji Kobayashi, Hong Sun & Hui Zhang
doi:10.1038/ncb1490
First Paragraph - | Full Text - CUL4–DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation | PDF (622 KB) - CUL4–DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation | Supplementary information
Control of Rad52 recombination activity by double-strand break-induced SUMO modification - pp1284 - 1290
Meik Sacher, Boris Pfander, Carsten Hoege & Stefan Jentsch
doi:10.1038/ncb1488
First Paragraph - | Full Text - Control of Rad52 recombination activity by double-strand break-induced SUMO modification | PDF (2,561 KB) - Control of Rad52 recombination activity by double-strand break-induced SUMO modification | Supplementary information
Mitogenic signalling and the p16INK4a–Rb pathway cooperate to enforce irreversible cellular senescence - pp1291 - 1297
Akiko Takahashi, Naoko Ohtani, Kimi Yamakoshi, Shin-ichi Iida, Hidetoshi Tahara, Keiko Nakayama, Keiichi I. Nakayama, Toshinori Ide, Hideyuki Saya & Eiji Hara
doi:10.1038/ncb1491
First Paragraph - | Full Text - Mitogenic signalling and the p16INK4a–Rb pathway cooperate to enforce irreversible cellular senescence | PDF (2,043 KB) - Mitogenic signalling and the p16INK4a–Rb pathway cooperate to enforce irreversible cellular senescence | Supplementary information
See also: News and Views by Ramsey & Sharpless
Input from Ras is required for maximal PI(3)K signalling in Drosophila - pp1298 - 1302
Mariam H. Orme, Saif Alrubaie, Gemma L. Bradley, Cherryl D. Walker & Sally J. Leevers
doi:10.1038/ncb1493
First Paragraph - | Full Text - Input from Ras is required for maximal PI(3)K signalling in Drosophila | PDF (823 KB) - Input from Ras is required for maximal PI(3)K signalling in Drosophila | Supplementary information
G
s and the Ras binding domain of p110
are both important regulators of PI3K
signalling in neutrophils - pp1303 - 1309
Sabine Suire, Alison M. Condliffe, G. John Ferguson, Chris D. Ellson, Hervé Guillou, Keith Davidson, Heidi Welch, John Coadwell, Martin Turner, Edwin R. Chilvers, Phillip T. Hawkins & Len Stephens
doi:10.1038/ncb1494
First Paragraph - | Full Text - G
s and the Ras binding domain of p110
are both important regulators of PI3K
signalling in neutrophils | PDF (998 KB) - G
s and the Ras binding domain of p110
are both important regulators of PI3K
signalling in neutrophils | Supplementary information


