Table of contents
From the editors
p1 | doi:10.1038/nrm2315
Research Highlights
Endocytosis: A new way to hijack the cell | PDF (242 KB)
p2 | doi:10.1038/nrm2318
Proteomics: Solving a 3D jigsaw puzzle | PDF (194 KB)
p3 | doi:10.1038/nrm2316
Molecular motors: Power in numbers | PDF (124 KB)
p4 | doi:10.1038/nrm2322
DNA replication: Wakey wakey! | PDF (133 KB)
p4 | doi:10.1038/nrm2325
Structure Watch
'Fight or flight' receptor revealed | PDF (96 KB)
p4 | doi:10.1038/nrm2326
In the news
Cloned monkeys yield stem cells | PDF (85 KB)
p5 | doi:10.1038/nrm2311
Stem cells: Ringing the changes | PDF (135 KB)
p6 | doi:10.1038/nrm2314
DNA damage: Conducting repair | PDF (173 KB)
p6 | doi:10.1038/nrm2323
In brief
Stem cells | Circadian rhythms | Transcription | Small RNAs | PDF (101 KB)
p7 | doi:10.1038/nrm2324
An Interview With...
Sydney Brenner | PDF (236 KB)
p8 | doi:10.1038/nrm2320
Reviews
Article series: Stem cells
No place like home: anatomy and function of the stem cell niche
D. Leanne Jones & Amy J. Wagers
p11 | doi:10.1038/nrm2319
The balance between stem cell self-renewal and differentiation is ultimately controlled by the integration of intrinsic factors with extrinsic cues supplied by the surrounding microenvironment, known as the stem cell niche. How much do we know about this intriguing microenvironment?
Argonaute proteins: key players in RNA silencing
Gyorgy Hutvagner & Martin J. Simard
p22 | doi:10.1038/nrm2321
The family of Argonaute proteins has important roles in RNA-mediated gene silencing. Argonaute proteins form complexes with small non-coding RNAs such as small interfering RNAs and microRNAs, control protein synthesis and mRNA stability, and participate in the production of a new class of small RNAs, Piwi-interacting RNAs.
Molecular architecture of the kinetochore–microtubule interface
Iain M. Cheeseman & Arshad Desai
p33 | doi:10.1038/nrm2310
Kinetochores are large proteinaceous structures that link centromeric DNA to spindle microtubules. More than 80 kinetochore proteins have been identified so far, and recent analyses are revealing how these proteins function to direct kinetochore specification and assembly, bind to microtubules and regulate chromosome segregation.
The BCL-2 protein family: opposing activities that mediate cell death
Richard J. Youle & Andreas Strasser
p47 | doi:10.1038/nrm2308
BCL-2 family proteins have either pro- or anti-apoptotic activities that are crucial for the regulation of apoptosis, tumorigenesis and cellular responses to anti-cancer therapy. Recent advances suggest that interactions between BCL-2 family proteins affect their localization and conformation and regulate their bioactivity.
Heterotrimeric G protein activation by G-protein-coupled receptors
William M. Oldham & Heidi E. Hamm
p60 | doi:10.1038/nrm2299
Extracellular signals can be transduced across the plasma membrane by activating G-protein-coupled receptors. The conformational changes induced in the receptor on ligand binding and how this causes the activation of the associated G protein are beginning to be understood.
Regulation of iron acquisition and storage: consequences for iron-linked disorders
Ivana De Domenico, Diane McVey Ward & Jerry Kaplan
p72 | doi:10.1038/nrm2295
Mammalian iron homeostasis is achieved through iron acquisition and storage. Intestinal iron absorption and macrophage-mediated recycling of iron from red blood cells are highly regulated. The discovery of iron transporters and insight into their regulation has provided important information about iron-related disorders.
Perspective
Article series: Stem cells
OPINION
Epidermal homeostasis: do committed progenitors work while stem cells sleep?
Philip Jones & Benjamin D. Simons
p82 | doi:10.1038/nrm2292
Studies of epidermis in vivo have revealed that a committed progenitor cell population can maintain normal adult tissue in the long term without support from a stem-cell population. Here, the stem-cell theories that explain epidermal homeostasis are challenged.
Corrigendum: When cilia go bad: cilia defects and ciliopathies
Manfred Fliegauf, Thomas Benzing & Heymut Omran
p88 | doi:10.1038/nrm2317


