Declaration of financial interests - ppE219 - E220

doi:10.1038/ncb1001-e219

Full Text - Declaration of financial interests | PDF (71 KB) - Declaration of financial interests

Presenilins and the intramembrane proteolysis of proteins: facts and fiction - ppE221 - E225

Bart De Strooper & Wim Annaert

doi:10.1038/ncb1001-e221

Missense mutations in the genes coding for presenilin 1 and presenilin 2 cause familial Alzheimer's disease — a progressive neurodegenerative disorder of the central nervous system. Loss-of-function mutations of these genes in Drosophila, Caenorhabditis elegans and mice cause severe lethal phenotypes, which implicates the presenilins genetically in the Notch signalling pathway. The hypothesis that presenilins are aspartyl proteases that cleave the amyloid precursor protein and Notch can explain the phenotypes. Direct evidence for this hypothesis is, however, difficult to obtain. Moreover, presenilin 1 is a multifunctional protein, as exemplified by its role in the Wnt/-catenin signalling pathway.

Full Text - Presenilins and the intramembrane proteolysis of proteins: facts and fiction | PDF (1,068 KB) - Presenilins and the intramembrane proteolysis of proteins: facts and fiction

Catch and pull a microtubule: getting a grasp on the cortex - ppE226 - E228

Viki Allan & Inke S. Näthke

doi:10.1038/ncb1001-e226

Cytoskeletal attachment to the cell cortex is crucial for mechanical and signalling events at the plasma membrane. The adenomatous polyposis coli (APC) protein, as well as -catenin in a complex with cytoplasmic dynein, is implicated in mediating such cortical attachment.

Full Text - Catch and pull a microtubule: getting a grasp on the cortex | PDF (1,553 KB) - Catch and pull a microtubule: getting a grasp on the cortex

See also: Brief Communication by Ligon et al.

Moving on up and down - pE228

Sarah Greaves

doi:10.1038/ncb1001-e228

Full Text - Moving on up and down | PDF (133 KB) - Moving on up and down

Sugar-coated pathways for developmental patterning - ppE229 - E231

Mark E. Fortini

doi:10.1038/ncb1001-e229

Signalling pathways controlling developmental cell fate rely on a variety of carbohydrate-based protein modifications, including glycosylation of cell-surface and extracellular-matrix proteins. Receptors themselves might be glycosylated during synthesis and secretory trafficking, regulating their subsequent signalling activities. Two recent reports have uncovered a shared requirement for nucleotide–sugar transport in these processes, underscoring the importance of carbohydrates in developmental patterning.

Full Text - Sugar-coated pathways for developmental patterning | PDF (6,233 KB) - Sugar-coated pathways for developmental patterning

Genetics still moving forward - pE231

Valerie Ferrier

doi:10.1038/ncb1001-e231

Full Text - Genetics still moving forward | PDF (173 KB) - Genetics still moving forward

Ubiquitination, proteasomes and GABA_A receptors - ppE232 - E233

Bernhard Lüscher & Cheryl A. Keller

doi:10.1038/ncb1001-e232

Inhibitory neurotransmission by -aminobutyric acid (GABA) is regulated by the number and subcellular localization of GABA_A receptors in the membrane of the target neuron. A new study suggests that the ubiquitin-like protein Plic-1 stabilizes intracellular GABA_A receptors and promotes their accumulation in the plasma membrane.

Full Text - Ubiquitination, proteasomes and GABAA receptors | PDF (372 KB) - Ubiquitination, proteasomes and GABAA receptors

The mystery of the centrosome - pE234

Robert Margolis reviews The Centrosome in Cell Replication and Early Development by Robert E. Palazzo & Gerald P. Schatten

doi:10.1038/ncb1001-e234

Full Text - The mystery of the centrosome | PDF (170 KB) - The mystery of the centrosome

Whatever the game is, play it as a professional - pE235

Ross L. Cagan reviews Winning the Games Scientists Play: Strategies for Enhancing Your Career in Science by Carl J. Sinderman

doi:10.1038/ncb1001-e235

Full Text - Whatever the game is, play it as a professional | PDF (168 KB) - Whatever the game is, play it as a professional

The art of the comprehensible - pE236

Simon L. Bullock reviews Effective Communication for Science and Technology by Joan van Emden

doi:10.1038/ncb1001-e236

Full Text - The art of the comprehensible | PDF (185 KB) - The art of the comprehensible

Molecular chaperone targeting and regulation by BAG family proteins - ppE237 - E241

Shinichi Takayama & John C. Reed

doi:10.1038/ncb1001-e237

Abstract - | Full Text - Molecular chaperone targeting and regulation by BAG family proteins | PDF (370 KB) - Molecular chaperone targeting and regulation by BAG family proteins

Borg proteins control septin organization and are negatively regulated by Cdc42 - pp861 - 866

Gérard Joberty, Richard R. Perlungher, Peter J. Sheffield, Makoto Kinoshita, Makoto Noda, Timothy Haystead & Ian G. Macara

doi:10.1038/ncb1001-861

Abstract - | Full Text - Borg proteins control septin organization and are negatively regulated by Cdc42 | PDF (1,802 KB) - Borg proteins control septin organization and are negatively regulated by Cdc42

Endogenous nitric oxide mechanisms mediate the stretch dependence of Ca²⁺ release in cardiomyocytes - pp867 - 873

Martín G. Vila Petroff, Suhn Hee Kim, Salvatore Pepe, Chantal Dessy, Eduardo Marbán, Jean-Luc Balligand & Steven J. Sollott

doi:10.1038/ncb1001-867

Abstract - | Full Text - Endogenous nitric oxide mechanisms mediate the stretch dependence of Ca2+ release in cardiomyocytes | PDF (236 KB) - Endogenous nitric oxide mechanisms mediate the stretch dependence of Ca2+ release in cardiomyocytes | Supplementary information

A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation - pp874 - 882

Carolyn S. Sevier, John W. Cuozzo, Andrea Vala, Fredrik Åslund & Chris A. Kaiser

doi:10.1038/ncb1001-874

Abstract - | Full Text - A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation | PDF (409 KB) - A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation

Spatial control of the actin cytoskeleton in Drosophila epithelial cells - pp883 - 890

Buzz Baum & Norbert Perrimon

doi:10.1038/ncb1001-883

Abstract - | Full Text - Spatial control of the actin cytoskeleton in Drosophila epithelial cells | PDF (5,391 KB) - Spatial control of the actin cytoskeleton in Drosophila epithelial cells

Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability - pp891 - 896

Felix Randow & Brian Seed

doi:10.1038/ncb1001-891

Abstract - | Full Text - Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability | PDF (334 KB) - Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility - pp897 - 904

Scott B. Snapper, Fuminao Takeshima, Inés Antón, Ching-Hui Liu, Sheila M. Thomas, Deanna Nguyen, Darryll Dudley, Hunter Fraser, Daniel Purich, Marco Lopez-Ilasaca, Christoph Klein, Laurie Davidson, Roderick Bronson, Richard C. Mulligan, Fred Southwick, Raif Geha, Marcia B. Goldberg, Fred S. Rosen, John H. Hartwig & Frederick W. Alt

doi:10.1038/ncb1001-897

Abstract - | Full Text - N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility | PDF (1,749 KB) - N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility | Supplementary information

Acyl-coenzyme A: cholesterol acyltransferase modulates the generation of the amyloid -peptide - pp905 - 912

Luigi Puglielli, Genevieve Konopka, Eunju Pack-Chung, Laura A. MacKenzie Ingano, Oksana Berezovska, Bradley T. Hyman, Ta Yuan Chang, Rudolph E. Tanzi & Dora M. Kovacs

doi:10.1038/ncb1001-905

Abstract - | Full Text - Acyl-coenzyme A: cholesterol acyltransferase modulates the generation of the amyloid -peptide | PDF (249 KB) - Acyl-coenzyme A: cholesterol acyltransferase modulates the generation of the amyloid -peptide

Dynein binds to -catenin and may tether microtubules at adherens junctions - pp913 - 917

Lee A. Ligon, Sher Karki, Mariko Tokito & Erika L. F. Holzbaur

doi:10.1038/ncb1001-913

Abstract - | Full Text - Dynein binds to -catenin and may tether microtubules at adherens junctions | PDF (884 KB) - Dynein binds to -catenin and may tether microtubules at adherens junctions

See also: News and Views by Allan & Näthke

Extracellular control of cell size - pp918 - 921

Ian J. Conlon, Graham A. Dunn, Anne W. Mudge & Martin C. Raff

doi:10.1038/ncb1001-918

Abstract - | Full Text - Extracellular control of cell size | PDF (290 KB) - Extracellular control of cell size | Supplementary information

Three-dimensional reconstruction of dynamin in the constricted state - pp922 - 926

Peijun Zhang & Jenny E. Hinshaw

doi:10.1038/ncb1001-922

Abstract - | Full Text - Three-dimensional reconstruction of dynamin in the constricted state | PDF (1,165 KB) - Three-dimensional reconstruction of dynamin in the constricted state | Supplementary information

Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP - pp927 - 932

Natasha K. Hussain, Sarah Jenna, Michael Glogauer, Christopher C. Quinn, Sylwia Wasiak, Michel Guipponi, Stylianos E. Antonarakis, Brian K. Kay, Thomas P. Stossel, Nathalie Lamarche-Vane & Peter S. McPherson

doi:10.1038/ncb1001-927

Abstract - | Full Text - Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP | PDF (1,786 KB) - Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP | Supplementary information

Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin - pp933 - 938

Brooke M. McCartney, Donald G. McEwen, Elizabeth Grevengoed, Paul Maddox, Amy Bejsovec & Mark Peifer

doi:10.1038/ncb1001-933

Abstract - | Full Text - Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin | PDF (4,205 KB) - Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin | Supplementary information

Proteins containing the UBA domain are able to bind to multi-ubiquitin chains - pp939 - 943

Caroline R.M. Wilkinson, Michael Seeger, Rasmus Hartmann-Petersen, Miranda Stone, Mairi Wallace, Colin Semple & Colin Gordon

doi:10.1038/ncb1001-939

Abstract - | Full Text - Proteins containing the UBA domain are able to bind to multi-ubiquitin chains | PDF (426 KB) - Proteins containing the UBA domain are able to bind to multi-ubiquitin chains | Supplementary information