Table of contents
August 2005, Volume 7 No 8 pp725-843
About the coverFocus
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The ubiquitin-proteasome system controls many cellular processes either by proteolytic or non-proteolytic means. The August 2005 issue of Nature Cell Biology presents a series of specially commissioned Reviews and Perspectives highlighting new insights into this pathway. The Focus is sponsored by Millennium Pharmaceuticals and Boston Biochem. |
Editorial
Focus on The Ubiquitin-Proteasome System
Focusing on the ubiquitin–proteasome system - p725
doi:10.1038/ncb0805-725
Full Text - Focusing on the ubiquitin–proteasome system | PDF (112 KB) - Focusing on the ubiquitin–proteasome system
Perspectives
Focus on The Ubiquitin-Proteasome System
Proteolysis: anytime, any place, anywhere? - pp731 - 735
Jonathon Pines & Catherine Lindon
doi:10.1038/ncb0805-731
Abstract - | Full Text - Proteolysis: anytime, any place, anywhere? | PDF (237 KB) - Proteolysis: anytime, any place, anywhere?
Focus on The Ubiquitin-Proteasome System
Protein quality control: chaperones culling corrupt conformations - pp736 - 741
Amie J. McClellan, Stephen Tam, Daniel Kaganovich & Judith Frydman
doi:10.1038/ncb0805-736
Abstract - | Full Text - Protein quality control: chaperones culling corrupt conformations | PDF (349 KB) - Protein quality control: chaperones culling corrupt conformations
Reviews
Focus on The Ubiquitin-Proteasome System
Delivery of ubiquitinated substrates to protein-unfolding machines - pp742 - 749
Suzanne Elsasser & Daniel Finley
doi:10.1038/ncb0805-742
Abstract - | Full Text - Delivery of ubiquitinated substrates to protein-unfolding machines | PDF (342 KB) - Delivery of ubiquitinated substrates to protein-unfolding machines | Supplementary information
Focus on The Ubiquitin-Proteasome System
Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics - pp750 - 757
Donald S. Kirkpatrick, Carilee Denison & Steven P. Gygi
doi:10.1038/ncb0805-750
Abstract - | Full Text - Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics | PDF (352 KB) - Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics
Focus on The Ubiquitin-Proteasome System
Ubiquitin signalling in the NF-
B pathway - pp758 - 765
Zhijian J. Chen
doi:10.1038/ncb0805-758
Abstract - | Full Text - Ubiquitin signalling in the NF-
B pathway | PDF (478 KB) - Ubiquitin signalling in the NF-
B pathway | Supplementary information
Focus on The Ubiquitin-Proteasome System
ERAD: the long road to destruction - pp766 - 772
Birgit Meusser, Christian Hirsch, Ernst Jarosch & Thomas Sommer
doi:10.1038/ncb0805-766
Abstract - | Full Text - ERAD: the long road to destruction | PDF (374 KB) - ERAD: the long road to destruction
News and Views
Substrate specificity: PI(3)K
has it both ways - pp773 - 774
Jonathan M. Backer
doi:10.1038/ncb0805-773
Phosphoinositide 3-kinases (PI(3)Ks) are mainly known for their lipid kinase activity in various cellular functions; however, PI(3)Ks also have protein kinase activity. Non-muscle tropomyosin has been identified as a novel protein target for PI(3)K
. Phosphorylation of tropomyosin is required for
-adrenergic receptor internalization, providing new insight into PI(3)K function during clathrin-mediated endocytosis.
Full Text - Substrate specificity: PI(3)K
has it both ways | PDF (181 KB) - Substrate specificity: PI(3)K
has it both ways
An actin fishnet for DNA - pp775 - 776
Ann L. Miller & William M. Bement
doi:10.1038/ncb0805-775
It has long been thought that gathering chromosomes during spindle assembly is exclusively the responsibility of microtubules. However, a recent study by Lénárt et al. shows that, in larger cells, a collapsing network of actin filaments ensnares and transports the chromosomes, bringing them in range for microtubule capture.
Full Text - An actin fishnet for DNA | PDF (171 KB) - An actin fishnet for DNA
Rac and cell migration: CDM proteins integrate signals - pp777 - 778
Henry R. Bourne
doi:10.1038/ncb0805-777
Cell migration requires that Rac GTPases promote formation of actin polymers at the cell's leading edge. An activator of Rac, DOCK180, accomplishes this localization by using its DHR-1 domain to bind phosphatidylinositol-3,4,5-trisphosphate at the membrane.
Full Text - Rac and cell migration: CDM proteins integrate signals | PDF (165 KB) - Rac and cell migration: CDM proteins integrate signals
Cdk1: the dominant sibling of Cdk2 - pp779 - 781
Tarig Bashir & Michele Pagano
doi:10.1038/ncb0805-779
Cdk2 is thought to regulate entry into S phase, whereas Cdk1 controls the initiation of mitosis. New evidence shows that Cdk1 is equally capable of promoting the G1/S transition in Cdk2-/- cells, raising the question as to whether Cdk1 constitutes the predominant cyclin-dependent kinase in mammalian cells, or only compensates for Cdk2 function when it is compromised.
Full Text - Cdk1: the dominant sibling of Cdk2 | PDF (310 KB) - Cdk1: the dominant sibling of Cdk2
MicroRNAs diversify in Drosophila development - p781
Alison Schuldt
doi:10.1038/ncb0805-781
Full Text - MicroRNAs diversify in Drosophila development | PDF (251 KB) - MicroRNAs diversify in Drosophila development
Book Review
Becoming a cell voyeur - p783
Julie C. Canman reviews Live Cell Imaging: A Laboratory Manual by Robert Goldman & David Spector
doi:10.1038/ncb0805-783
Full Text - Becoming a cell voyeur | PDF (119 KB) - Becoming a cell voyeur
Articles
Protein kinase activity of phosphoinositide 3-kinase regulates
-adrenergic receptor endocytosis - pp785 - 796
Sathyamangla V. Naga Prasad, Arundathi Jayatilleke, Aasakiran Madamanchi & Howard A. Rockman
doi:10.1038/ncb1278
Abstract - | Full Text - Protein kinase activity of phosphoinositide 3-kinase regulates
-adrenergic receptor endocytosis | PDF (1,909 KB) - Protein kinase activity of phosphoinositide 3-kinase regulates
-adrenergic receptor endocytosis | Supplementary information
See also: News and Views by Backer
A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling - pp797 - 807
Jean-François Côté, Andrea B. Motoyama, Jason A. Bush & Kristiina Vuori
doi:10.1038/ncb1280
Abstract - | Full Text - A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling | PDF (1,302 KB) - A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling | Supplementary information
See also: News and Views by Bourne
Membrane phosphatidylserine distribution as a non-apoptotic signalling mechanism in lymphocytes - pp808 - 816
James I. Elliott, Annmarie Surprenant, Federica M. Marelli-Berg, Joanne C. Cooper, Robin L. Cassady-Cain, Carol Wooding, Kenneth Linton, Denis R. Alexander & Christopher F. Higgins
doi:10.1038/ncb1279
Abstract - | Full Text - Membrane phosphatidylserine distribution as a non-apoptotic signalling mechanism in lymphocytes | PDF (1,142 KB) - Membrane phosphatidylserine distribution as a non-apoptotic signalling mechanism in lymphocytes | Supplementary information
Letters
Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol - pp817 - 822
Harald W. Platta, Silke Grunau, Katja Rosenkranz, Wolfgang Girzalsky & Ralf Erdmann
doi:10.1038/ncb1281
First Paragraph - | Full Text - Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol | PDF (513 KB) - Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol | Supplementary information
Temporal and spatial control of nucleophosmin by the Ran–Crm1 complex in centrosome duplication - pp823 - 830
Wei Wang, Anuradha Budhu, Marshonna Forgues & Xin Wei Wang
doi:10.1038/ncb1282
First Paragraph - | Full Text - Temporal and spatial control of nucleophosmin by the Ran–Crm1 complex in centrosome duplication | PDF (744 KB) - Temporal and spatial control of nucleophosmin by the Ran–Crm1 complex in centrosome duplication | Supplementary information
Cdc2–cyclin E complexes regulate the G1/S phase transition - pp831 - 836
Eiman Aleem, Hiroaki Kiyokawa & Philipp Kaldis
doi:10.1038/ncb1284
First Paragraph - | Full Text - Cdc2–cyclin E complexes regulate the G1/S phase transition | PDF (2,176 KB) - Cdc2–cyclin E complexes regulate the G1/S phase transition | Supplementary information
See also: News and Views by Bashir & Pagano
Prohibitin is required for Ras-induced Raf–MEK–ERK activation and epithelial cell migration - pp837 - 843
Krishnaraj Rajalingam, Christian Wunder, Volker Brinkmann, Yuri Churin, Mirko Hekman, Claudia Sievers, Ulf R. Rapp & Thomas Rudel
doi:10.1038/ncb1283
First Paragraph - | Full Text - Prohibitin is required for Ras-induced Raf–MEK–ERK activation and epithelial cell migration | PDF (752 KB) - Prohibitin is required for Ras-induced Raf–MEK–ERK activation and epithelial cell migration | Supplementary information


