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

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

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

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

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

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

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