Table of contents
From the Editors
p703 | doi:10.1038/nrm2038
Research Highlights
Gene regulation: Welded on the spot
p705 | doi:10.1038/nrm2033
Mechanisms of disease: Perils of ageing
p706 | doi:10.1038/nrm2029
Mitosis: Give us a kiz
p706 | doi:10.1038/nrm2032
Imaging: Overcoming the barrier
p707 | doi:10.1038/nrm2027
Ageing: Balancing self-renewal and ageing
p708 | doi:10.1038/nrm2036
Chromatin: Eukaryotic genomes in complete control
p709 | doi:10.1038/nrm2035
Chromatin: The yin and yang...
p710 | doi:10.1038/nrm2028
Membrane trafficking: Kiss and patch up
p710 | doi:10.1038/nrm2031
In the news
Hitting junk
p710 | doi:10.1038/nrm2040
Reviews
The ARP2/3 complex: an actin nucleator comes of age
Erin D. Goley and Matthew D. Welch
p713 | doi:10.1038/nrm2026
The ARP2/3 complex regulates the initiation of actin polymerization and the organization of filaments into y-branched networks. Recent studies have begun to reveal the role of this complex in diverse cellular processes and its molecular mechanisms of action, as well as its misregulation during disease.
The COPII cage: unifying principles of vesicle coat assembly
Cemal Gürkan, Scott M. Stagg, Paul LaPointe and William E. Balch
p727 | doi:10.1038/nrm2025
Recent studies of the early secretory pathway have analysed cargo selection and transport-carrier formation by components of the endoplasmic-reticulum-associated coat protein complex-II (COPII). Results are indicative of a unifying model of cage and coat function in vesicle and tubule formation as well as fission in endomembrane traffic.
Mechanism of homologous recombination: mediators and helicases take on regulatory functions
Patrick Sung and Hannah Klein
p739 | doi:10.1038/nrm2008
Homologous recombination has an important role in DNA repair, DNA replication, meiotic chromosome segregation and telomere maintenance. Its tight regulation by DNA helicases and mediator proteins is essential to avoid cell-cycle arrest, genome destabilization and cancer formation.
The replication clamp-loading machine at work in the three domains of life
Chiara Indiani and Mike O'Donnell
p751 | doi:10.1038/nrm2022
Processive DNA polymerases that replicate chromosomes interact with a ring-shaped clamp that encircles DNA and slides along the duplex. The sliding clamp is loaded onto DNA by a clamp-loader complex. Structural and biochemical studies have provided mechanistic insights into the clamp-loading process.
Article series: Mechanisms of disease
Molecular mechanisms of muscular dystrophies: old and new players
Kay E Davies and Kristen J Nowak
p762 | doi:10.1038/nrm2024
The study of muscular dystrophies has shown that mutant proteins result in perturbations of many cellular components. These findings have revealed important insights for cell biologists, and have also identified unexpected and exciting new approaches for therapy.
Perspectives
Innovation
A chemical toolkit for proteins — an expanded genetic code
Jianming Xie and Peter G. Schultz
p775 | doi:10.1038/nrm2005
Recently, a method was developed to encode unnatural amino acids genetically in bacteria, yeast and mammalian cells. This provides a powerful tool for exploring protein structure and function in vitro and in vivo, and for generating proteins with new or enhanced properties.
Opinion
SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton
Yonatan B. Tzur, Katherine L. Wilson and Yosef Gruenbaum
p782 | doi:10.1038/nrm2003
The SUN-domain family of nuclear envelope proteins interacts with KASH-domain proteins, which are also nuclear envelope proteins, to form 'bridges' across the inner and outer nuclear membranes. SUN-domain proteins are now proposed to provide a mechanical connection between the nucleoskeleton and the cytoskeleton.
