Advance online publication
The latest research papers, published online ahead of print. These online versions are definitive and may be cited using the digital object identifier (DOI).
About advance online publicationArticles
AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling
Saumya Pant, Mahak Sharma, Kruti Patel, Steve Caplan, Chavela M. Carr & Barth D. Grant
Published online: 15 November 2009 | doi:10.1038/ncb1986
The RME1 ATPases are implicated in endocytic recycling. C. elegans RME1 interacts with Amphiphysin to regulate endocytic recycling in vivo and the two proteins cooperate in the generation of cargo carriers in vitro. The interaction is conserved in other eukaryotes.
Abstract - AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling | Full Text - AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling | PDF (4,500 KB) - AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling | Supplementary information
The let-7 target gene mouse lin-41 is a stem cell specific E3 ubiquitin ligase for the miRNA pathway protein Ago2
Agnieszka Rybak, Heiko Fuchs, Kamyar Hadian, Lena Smirnova, Ellery A. Wulczyn, Geert Michel, Robert Nitsch, Daniel Krappmann & F. Gregory Wulczyn
Published online: 08 November 2009 | doi:10.1038/ncb1987
Let-7 microRNA (miRNA) and its target gene lin-28 regulate pluripotency. A second Let-7 target, lin-41, controls miRNA function in stem cells by regulating the turnover of the miRNA effector Argonaute2 through its ubiquitin ligase activity.
Abstract - The let-7 target gene mouse : lin-41: is a stem cell specific E3 ubiquitin ligase for the miRNA pathway protein Ago2 | Full Text - The let-7 target gene mouse lin-41 is a stem cell specific E3 ubiquitin ligase for the miRNA pathway protein Ago2 | PDF (5,418 KB) - The let-7 target gene mouse lin-41 is a stem cell specific E3 ubiquitin ligase for the miRNA pathway protein Ago2 | Supplementary information
Letters
M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complex
Koji Hase, Shunsuke Kimura, Hiroyuki Takatsu, Masumi Ohmae, Sayaka Kawano, Hiroshi Kitamura, Masatoshi Ito, Hiroshi Watarai, C. Clayton Hazelett, Charles Yeaman & Hiroshi Ohno
Published online: 22 November 2009 | doi:10.1038/ncb1990
How tunnelling nanotubes form between cells is unclear. A mammalian protein, M-Sec, that has homology to the Sec6 subunit of the exocyst complex, is sufficient and necessary for nanotube formation. The Ral GTPase and its effector, the exocyst complex, are required for M-Sec-dependent regulation of nanotubes.
First Paragraph - M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complex | Full Text - M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complex | PDF (5,161 KB) - M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complex | Supplementary information
The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-inhibiting microRNAs
Ulrich Wellner, Jörg Schubert, Ulrike C. Burk, Otto Schmalhofer, Feng Zhu, Annika Sonntag, Bettina Waldvogel, Corinne Vannier, Douglas Darling, Axel zur Hausen, Valerie G. Brunton, Jennifer Morton, Owen Sansom, Julia Schüler, Marc P. Stemmler, Christoph Herzberger, Ulrich Hopt, Tobias Keck, Simone Brabletz & Thomas Brabletz
Published online: 22 November 2009 | doi:10.1038/ncb1998
The epithelial-to-mesenchymal transition transcription factor ZEB1 is involved in metastasis. It is now shown to regulate the tumour-initiating capacity of pancreatic and colorectal cancer cells, through the repression of the stemness-inhibiting miR200s, which are found to inhibit the polycomb repressor Bmi-1.
First Paragraph - The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-inhibiting microRNAs | Full Text - The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-inhibiting microRNAs | PDF (1,980 KB) - The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-inhibiting microRNAs | Supplementary information
YAP-dependent induction of amphiregulin identifies a non-cell-autonomous component of the Hippo pathway
Jianmin Zhang, Jun-Yuan Ji, Min Yu, Michael Overholtzer, Gromoslaw A. Smolen, Rebecca Wang, Joan S. Brugge, Nicholas J. Dyson & Daniel A. Haber
Published online: 22 November 2009 | doi:10.1038/ncb1993
The Hippo pathway regulates proliferation and survival in Drosophila and mammals, although shared transcriptional targets of their effectors have not been identified. Mammalian YAP controls expression of the EGFR ligand amphiregulin to regulate epithelial-to-mesenchymal transition in mammary epithelial cells, and the EGFR pathway genetically interacts with Yorkie in Drosophila.
First Paragraph - YAP-dependent induction of amphiregulin identifies a non-cell-autonomous component of the Hippo pathway | Full Text - YAP-dependent induction of amphiregulin identifies a non-cell-autonomous component of the Hippo pathway | PDF (2,389 KB) - YAP-dependent induction of amphiregulin identifies a non-cell-autonomous component of the Hippo pathway | Supplementary information
Cell fate decisions are specified by the dynamic ERK interactome
Alex von Kriegsheim, Daniela Baiocchi, Marc Birtwistle, David Sumpton, Willy Bienvenut, Nicholas Morrice, Kayo Yamada, Angus Lamond, Gabriella Kalna, Richard Orton, David Gilbert & Walter Kolch
Published online: 22 November 2009 | doi:10.1038/ncb1994
In differentiating cells, ERK activation shifts from transient to sustained. Quantitative proteomics reveals that, during differentiation, dynamic changes in ERK-interacting proteins regulate the pathway at several levels and by different mechanisms, suggesting a distributed control mechanism for the ERK pathway.
First Paragraph - Cell fate decisions are specified by the dynamic ERK interactome | Full Text - Cell fate decisions are specified by the dynamic ERK interactome | PDF (3,059 KB) - Cell fate decisions are specified by the dynamic ERK interactome | Supplementary information
Adaptive force transmission in amoeboid cell migration
Jörg Renkawitz, Kathrin Schumann, Michele Weber, Tim Lämmermann, Holger Pflicke, Matthieu Piel, Julien Polleux, Joachim P. Spatz & Michael Sixt
Published online: 15 November 2009 | doi:10.1038/ncb1992
Migrating dendritic cells can adapt their adhesive properties to switch between integrin-dependent and -independent modes of migration. By modulating their actin polymerization dynamics, cells can maintain a steady migration speed through a changing environment.
First Paragraph - Adaptive force transmission in amoeboid cell migration | Full Text - Adaptive force transmission in amoeboid cell migration | PDF (3,694 KB) - Adaptive force transmission in amoeboid cell migration | Supplementary information
A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor–promoter DNA complex
Alexander J. Wilcox & Jeffrey D. Laney
Published online: 15 November 2009 | doi:10.1038/ncb1997
Yeast mating-type switching requires ubiquitylation of the transcriptional repressor 
2. This results in removal of 2 from its DNA targets by the ubiquitin-selective AAA-ATPase Cdc48, thus revealing a nuclear function of Cdc48 and an ubiquitin-dependent extraction pathway for dismantling transcription factor—DNA complexes.
First Paragraph - A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor-promoter DNA complex | Full Text - A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor–promoter DNA complex | PDF (1,149 KB) - A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor–promoter DNA complex | Supplementary information
TAp63 induces senescence and suppresses tumorigenesis in vivo
Xuecui Guo, William M. Keyes, Cristian Papazoglu, Johannes Zuber, Wangzhi Li, Scott W. Lowe, Hannes Vogel & Alea A. Mills
Published online: 08 November 2009 | doi:10.1038/ncb1988
TAp63, a splice variant of the p53 homologue p63, suppresses tumorigenesis in p53-null mice by mediating Ras oncogene-induced senescence. TAp63-mediated senescence is independent of p53, but requires p21Waf/Cip1 and Rb. TAp63 overrides Ras-driven transformation, while its loss accelerates Ras oncogenesis.
First Paragraph - TAp63 induces senescence and suppresses tumorigenesis : in vivo | Full Text - TAp63 induces senescence and suppresses tumorigenesis in vivo | PDF (2,588 KB) - TAp63 induces senescence and suppresses tumorigenesis in vivo | Supplementary information
A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation
Mitsuko Hayashi-Nishino, Naonobu Fujita, Takeshi Noda, Akihito Yamaguchi, Tamotsu Yoshimori & Akitsugu Yamamoto
Published online: 08 November 2009 | doi:10.1038/ncb1991
Autophagy is a bulk degradation process that takes place in specialized membrane structures, the origin of which is still unclear. An electron tomography study shows that the ER is connected to the isolation membranes that initiate autophagosome formation in mammalian cells, suggesting that the ER is the membrane source.
First Paragraph - A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation | Full Text - A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation | PDF (5,574 KB) - A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation | Supplementary information
Regulation of a Golgi flippase by phosphoinositides and an ArfGEF
Paramasivam Natarajan, Ke Liu, Dustin V. Patil, Vicki A. Sciorra, Catherine L. Jackson & Todd R. Graham
Published online: 08 November 2009 | doi:10.1038/ncb1989
Drs2, a phospholipid translocase involved in transport from the trans-Golgi network, is shown to be a new effector of PtdIns(4)P (phosphatidylinositol 4-phosphate). Binding to PtdIns(4)P and to the GTPase exchange factor ARF–GEF, a regulator of Golgi transport, stimulates Drs2 activity.
First Paragraph - Regulation of a Golgi flippase by phosphoinositides and an ArfGEF | Full Text - Regulation of a Golgi flippase by phosphoinositides and an ArfGEF | PDF (1,512 KB) - Regulation of a Golgi flippase by phosphoinositides and an ArfGEF | Supplementary information
Phosphorylation of STIM1 underlies suppression of store-operated calcium entry during mitosis
Jeremy T. Smyth, John G. Petranka, Rebecca R. Boyles, Wayne I. DeHaven, Miwako Fukushima, Katina L. Johnson, Jason G. Williams & James W. Putney Jr
Published online: 01 November 2009 | doi:10.1038/ncb1995
During mitosis, store-operated Ca2+ entry (SOCE) is suppressed. Translocation of the ER Ca2+ sensor STIM1 to the plasma membrane is critical to SOCE activation, but in mitotic cells STIM1 is phosphorylated and fails to rearrange into near-plasma membrane puncta. Mutation of mitosis-specific phosphorylation sites rescues mitotic SOCE.
First Paragraph - Phosphorylation of STIM1 underlies suppression of store-operated calcium entry during mitosis | Full Text - Phosphorylation of STIM1 underlies suppression of store-operated calcium entry during mitosis | PDF (3,075 KB) - Phosphorylation of STIM1 underlies suppression of store-operated calcium entry during mitosis | Supplementary information
Adaptive suppression of the ATF4–CHOP branch of the unfolded protein response by toll-like receptor signalling
Connie W. Woo, Dongying Cui, Jerry Arellano, Bernhard Dorweiler, Heather Harding, Katherine A. Fitzgerald, David Ron & Ira Tabas
Published online: 25 October 2009 | doi:10.1038/ncb1996
Under prolonged ER stress, expression of the unfolded protein response effector CHOP becomes cytotoxic. Toll-like receptor engagement activates TRIF signalling to inhibit the translational activation of the UPR effector ATF4 and thus suppresses CHOP-associated cell death and organ dysfunction in mice.
First Paragraph - Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling | Full Text - Adaptive suppression of the ATF4–CHOP branch of the unfolded protein response by toll-like receptor signalling | PDF (2,347 KB) - Adaptive suppression of the ATF4–CHOP branch of the unfolded protein response by toll-like receptor signalling | Supplementary information
Until print versions of AOP papers are published, they should be cited in the style "Author(s) Nature Cell Biology advance online publication, day month year (doi:10.1038/ncbXXXXX)". Once the print version (identical to the AOP) is published, it should be cited as follows: "Author(s) Nature Cell Biology volume, page (year); advance online publication, (doi:10.1038/ncbXXXXX)".
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