Table of contents
October 2001, Volume 3 No 10 ppE219-943
About the coverEditorial
Declaration of financial interests - ppE219 - E220
doi:10.1038/ncb1001-e219
Full Text - Declaration of financial interests | PDF (71 KB) - Declaration of financial interests
Commentary
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
News and Views
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 GABAA 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 GABAA receptors in the membrane of the target neuron. A new study suggests that the ubiquitin-like protein Plic-1 stabilizes intracellular GABAA receptors and promotes their accumulation in the plasma membrane.
Full Text - Ubiquitination, proteasomes and GABAA receptors | PDF (372 KB) - Ubiquitination, proteasomes and GABAA receptors
Book Reviews
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
Review
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
Articles
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
Brief Communications
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


