Table of contents
March 2007 Vol 8 No 3
From the editors
p175 | doi:10.1038/nrm2037
Research Highlights
Stem cells: Fledglings escape from the niche
p177 | doi:10.1038/nrm2132
Post-translational modification: A smooth handover
p178 | doi:10.1038/nrm2123
Genome stability: A protective HAT
p178 | doi:10.1038/nrm2127
Cancer: PTEN — a new guardian of the genome
p179 | doi:10.1038/nrm2128
P53: A signalling integration node
p180 | doi:10.1038/nrm2133
Cell cycle: An unlikely pairing
p181 | doi:10.1038/nrm2121
Development: Reaching one's range
p181 | doi:10.1038/nrm2129
Development: Solving size issues
p182 | doi:10.1038/nrm2130
In the news
A distinct human signature
p182 | doi:10.1038/nrm2131
Development: Notch mediates the sprouting of tip cells
p182 | doi:10.1038/nrm2136
Reviews
The multiple faces of caveolae
Robert G. Parton and Kai Simons
p185 | doi:10.1038/nrm2122
Caveolae are highly abundant, but enigmatic, specialized membrane structures in mammalian cells. What might the function of these specialized domains be? Caveolae function as carriers in the exocytic and endocytic pathways, but have also been implicated in signalling, mechanosensing and lipid regulation.
Molecular mechanism of the nuclear protein import cycle
Murray Stewart
p195 | doi:10.1038/nrm2114
The classic nuclear protein import pathway comprises an organized cycle of interactions between cargoes and carrier proteins, and is powered by the Ran GTPases. Structural and functional data have uncovered the mechanisms of molecular recognition and the coordination of interactions in this pathway.
Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs
A. Gregory Matera, Rebecca M. Terns and Michael P. Terns
p209 | doi:10.1038/nrm2124
Recent studies have revealed remarkable complexity in the biogenesis, trafficking and mechanisms of action of small nuclear and small nucleolar ribonucleoproteins (RNPs). The principles of RNP-complex formation can be used to understand the regulation and function of other non-coding RNPs.
Matrix metalloproteinases and the regulation of tissue remodelling
Andrea Page-McCaw, Andrew J. Ewald and Zena Werb
p221 | doi:10.1038/nrm2125
New insights from mouse, Drosophila melanogaster and human studies have shed light on the functions of matrix metalloproteinases (MMPs) as active regulators of embryonic development, tissue remodelling and tissue repair in response to injury, infection or disease.
Emerging roles of nuclear protein phosphatases
Greg B. G. Moorhead, Laura Trinkle-Mulcahy and Annegret Ulke-Lemée
p234 | doi:10.1038/nrm2126
Large-scale approaches have linked protein phosphatase function to a multitude of nuclear processes, such as the DNA-damage response, cell-cycle progression and gene regulation. In addition, proteomics techniques have enabled the identification of new components of multiprotein phosphatase complexes, such as targeting and regulatory subunits.
In search of partners: linking extracellular proteases to substrates
Christopher M. Overall and Carl P. Blobel
p245 | doi:10.1038/nrm2120
Extracellular proteases regulate cell function through proteolytic switching of signalling circuits and through shedding of membrane proteins. It is crucial to link proteases to their substrates to understand their functions in development and disease, and to validate proteases as drug targets.
Perspective
Opinion
Sheets, ribbons and tubules — how organelles get their shape
Gia K. Voeltz and William A. Prinz
p258 | doi:10.1038/nrm2119
Organelles adopt many complex and dynamic shapes that are often conserved throughout evolution. We are only beginning to understand the mechanisms by which organelle shape is generated and maintained and how, even in the same organelle, different morphologies are created.
