Table of contents
March 2002, Volume 4 No 3 ppE45-260
About the coverEditorial
Cancer Research UK - pE45
doi:10.1038/ncb0302-e45
Full Text - Cancer Research UK | PDF (54 KB) - Cancer Research UK
Letters to Editor
Calcineurin and skeletal muscle growth - pE46
Shannon E. Dunn, Alain R. Simard, Renée A. Prud'homme & Robin N. Michel
doi:10.1038/ncb0302-e46a
Full Text - Calcineurin and skeletal muscle growth | PDF (535 KB) - Calcineurin and skeletal muscle growth
Reply: Calcineurin and skeletal muscle growth - ppE46 - E47
George D. Yancopoulos & David J. Glass
doi:10.1038/ncb0302-e46b
Full Text - Reply: Calcineurin and skeletal muscle growth | PDF (535 KB) - Reply: Calcineurin and skeletal muscle growth
Commentary
Selector and signalling molecules cooperate in organ patterning - ppE48 - E51
Jennifer Curtiss, Georg Halder & Marek Mlodzik
doi:ncb10.1038/ncb0302-e48
Cell signalling is essential for a plethora of inductive interactions during organogenesis. Surprisingly, only a few different classes of signalling molecules mediate many inductive interactions, and these molecules are used reiteratively during development. This raises the question of how generic signals can trigger tissue-specific responses. Recent studies in Drosophila melanogaster indicate that signalling molecules cooperate with selector genes to specify particular body parts and organ types. Selector and signalling inputs are integrated at the level of cis-regulatory elements, where direct binding of both selector proteins and signal transducers is required to activate tissue-specific enhancer elements of target genes. Such enhancers include autoregulatory enhancers of the selector genes themselves, which drive the refinement of expression patterns of selector genes.
Full Text - Selector and signalling molecules cooperate in organ patterning | PDF (196 KB) - Selector and signalling molecules cooperate in organ patterning
News and Views
Nuclear organization and silencing: putting things in their place - ppE53 - E55
Florence Hediger & Susan M. Gasser
doi:10.1038/ncb0302-e53
The positioning of a gene within the nucleus is thought to help regulate its transcriptional state. An example is yeast telomeres, which have a propensity to cluster at the nuclear periphery and suppress subtelomeric genes. With a membrane anchoring technique, new data indicate that there may be a second class of perinuclear silencing sites, which require pore-associated myosin-like proteins to establish repression.
Full Text - Nuclear organization and silencing: putting things in their place | PDF (359 KB) - Nuclear organization and silencing: putting things in their place
See also: Article by Feuerbach et al.
Intervening through interferon - pE55
Alison Schuldt
doi:10.1038/ncb0302-e55
Full Text - Intervening through interferon | PDF (184 KB) - Intervening through interferon
The ins and outs of polycystin-2 as a calcium release channel - ppE56 - E57
Michael D. Cahalan
doi:10.1038/ncb0302-e56
Mutations in either of two polycystin genes can cause kidney failure, but controversy remains regarding the cellular localization and function of the protein products. Polycystin-2 may be a calcium release channel located within the endoplasmic reticulum (ER), and yet may be physically linked to polycystin-1 in the surface membrane.
Full Text - The ins and outs of polycystin-2 as a calcium release channel | PDF (197 KB) - The ins and outs of polycystin-2 as a calcium release channel
See also: Article by Koulen et al.
Getting hit by SUMO - pE57
Valerie Ferrier
doi:10.1038/ncb0302-e57
Full Text - Getting hit by SUMO | PDF (130 KB) - Getting hit by SUMO
Many roads lead to the origin - ppE58 - E59
Domenico Maiorano & Marcel Méchali
doi:10.1038/ncb0302-e58
The assembly of the DNA helicase at replication origins is crucial in initiating DNA synthesis. This process requires the conserved protein Cdt1. Here, a new study identifies a functional homologue of Cdt1 in Saccharomyces cerevisiae. The regulation of its activity reveals an alternative way to assemble prereplicative complexes (pre-RCs) and regulate origin function.
Full Text - Many roads lead to the origin | PDF (189 KB) - Many roads lead to the origin
See also: Article by Tanaka & Diffley
Book Reviews
A practical prion protein primer - pE61
Adriano Aguzzi reviews Advances in Protein Chemistry: Prion Proteins by Byron Caughey
doi:10.1038/ncb0302-e61
Full Text - A practical prion protein primer | PDF (134 KB) - A practical prion protein primer
Physics of the cytoskeleton - pE62
Jonathan Scholey reviews Mechanics of Motor Proteins and the Cytoskeleton by Jonathan Howard
doi:10.1038/ncb0302-e62
Full Text - Physics of the cytoskeleton | PDF (119 KB) - Physics of the cytoskeleton
Articles
SMIF, a Smad4-interacting protein that functions as a co-activator in TGF
signalling - pp181 - 190
Ren-Yuan Bai, Christina Koester, Tao Ouyang, Stephan A. Hahn, Matthias Hammerschmidt, Christian Peschel & Justus Duyster
doi:10.1038/ncb753
Abstract - SMIF, a Smad4-interacting protein that functions as a co-activator in TGF[beta] signalling | Full Text - SMIF, a Smad4-interacting protein that functions as a co-activator in TGF
signalling | PDF (2,364 KB) - SMIF, a Smad4-interacting protein that functions as a co-activator in TGF
signalling |
Supplementary information
Polycystin-2 is an intracellular calcium release channel - pp191 - 197
Peter Koulen, Yiqiang Cai, Lin Geng, Yoshiko Maeda, Sayoko Nishimura, Ralph Witzgall, Barbara E. Ehrlich & Stefan Somlo
doi:10.1038/ncb754
Abstract - Polycystin-2 is an intracellular calcium release channel | Full Text - Polycystin-2 is an intracellular calcium release channel | PDF (350 KB) - Polycystin-2 is an intracellular calcium release channel
See also: News and Views by Cahalan
Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2–7 during G1 phase - pp198 - 207
Seiji Tanaka & John F.X. Diffley
doi:10.1038/ncb757
Abstract - Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2-7 during G1 phase | Full Text - Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2–7 during G1 phase | PDF (1,778 KB) - Interdependent nuclear accumulation of budding yeast Cdt1 and Mcm2–7 during G1 phase | Supplementary information
See also: News and Views by Maiorano & Méchali
A Drosophila APC tumour suppressor homologue functions in cellular adhesion - pp208 - 213
Fumihiko Hamada & Mariann Bienz
doi:10.1038/ncb755
Abstract - A : Drosophila: APC tumour suppressor homologue functions in cellular adhesion | Full Text - A Drosophila APC tumour suppressor homologue functions in cellular adhesion | PDF (1,828 KB) - A Drosophila APC tumour suppressor homologue functions in cellular adhesion
Nuclear architecture and spatial positioning help establish transcriptional states of telomeres in yeast - pp214 - 221
Frank Feuerbach, Vincent Galy, Edgar Trelles-Sticken, Micheline Fromont-Racine, Alain Jacquier, Eric Gilson, Jean-Christophe Olivo-Marin, Harry Scherthan & Ulf Nehrbass
doi:10.1038/ncb756
Abstract - Nuclear architecture and spatial positioning help establish transcriptional states of telomeres in yeast | Full Text - Nuclear architecture and spatial positioning help establish transcriptional states of telomeres in yeast | PDF (2,754 KB) - Nuclear architecture and spatial positioning help establish transcriptional states of telomeres in yeast | Supplementary information
See also: News and Views by Hediger & Gasser
Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex - pp222 - 231
Yasuyuki Fujita, Gerd Krause, Martin Scheffner, Dietmar Zechner, Hugo E. Molina Leddy, Jürgen Behrens, Thomas Sommer & Walter Birchmeier
doi:10.1038/ncb758
Abstract - Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex | Full Text - Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex | PDF (794 KB) - Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex | Supplementary information
Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI - pp232 - 239
Miguel Angel Del Pozo, William B. Kiosses, Nazilla B. Alderson, Nahum Meller, Klaus M. Hahn & Martin Alexander Schwartz
doi:10.1038/ncb759
Abstract - Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI | Full Text - Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI | PDF (2,218 KB) - Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI | Supplementary information
Brief Communications
Arfaptin 2 regulates the aggregation of mutant huntingtin protein - pp240 - 245
Peter J. Peters, Ke Ning, Felipe Palacios, Rita L. Boshans, Aleksey Kazantsev, Leslie M. Thompson, Ben Woodman, Gillian P. Bates & Crislyn D'Souza-Schorey
doi:10.1038/ncb761
Abstract - Arfaptin 2 regulates the aggregation of mutant huntingtin protein | Full Text - Arfaptin 2 regulates the aggregation of mutant huntingtin protein | PDF (2,481 KB) - Arfaptin 2 regulates the aggregation of mutant huntingtin protein | Supplementary information
Myosin-X is an unconventional myosin that undergoes intrafilopodial motility - pp246 - 250
Jonathan S. Berg & Richard E. Cheney
doi:10.1038/ncb762
Abstract - Myosin-X is an unconventional myosin that undergoes intrafilopodial motility | Full Text - Myosin-X is an unconventional myosin that undergoes intrafilopodial motility | PDF (940 KB) - Myosin-X is an unconventional myosin that undergoes intrafilopodial motility | Supplementary information
dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires dPDK1 - pp251 - 255
Thomas Radimerski, Jacques Montagne, Felix Rintelen, Hugo Stocker, Jeroen van der Kaay, C. Peter Downes, Ernst Hafen & George Thomas
doi:ncb10.1038/ncb763
Abstract - dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires dPDK1 | Full Text - dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires dPDK1 | PDF (602 KB) - dS6K-regulated cell growth is dPKB/dPI(3)K-independent, but requires dPDK1 | Supplementary information
Polyglycylation domain of
-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena - pp256 - 259
Rupal Thazhath, Chengbao Liu & Jacek Gaertig
doi:10.1038/ncb764
Abstract - Polyglycylation domain of [beta]-tubulin maintains axonemal architecture and affects cytokinesis in : Tetrahymena | Full Text - Polyglycylation domain of
-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena | PDF (1,637 KB) - Polyglycylation domain of
-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena


