Latest Articles Include:
- From the editors
- Nat Rev Mol Cell Biol 10(6):365 (2009)
- Chromatin: CENP-A on target
- Nat Rev Mol Cell Biol 10(6):367 (2009)
- Protein degradation: Tipping the balance
- Nat Rev Mol Cell Biol 10(6):368 (2009)
- Cell migration: Talin heads off
- Nat Rev Mol Cell Biol 10(6):368 (2009)
- Plant cell biology: New receptors for ABA
- Nat Rev Mol Cell Biol 10(6):368 (2009)
- In brief: Mitosis, Gene expression, Protein degradation, Polycomb proteins
- Nat Rev Mol Cell Biol 10(6):369 (2009)
- Protein degradation: Chain gang
- Nat Rev Mol Cell Biol 10(6):370 (2009)
- Technology Watch: Hunting phosphoproteins, See the force
- Nat Rev Mol Cell Biol 10(6):370 (2009)
- Post-translational modification: Examining the Fic domain
- Nat Rev Mol Cell Biol 10(6):371 (2009)
- DNA repair: Time to switch
- Nat Rev Mol Cell Biol 10(6):371 (2009)
- Prions: Prying into prions
- Nat Rev Mol Cell Biol 10(6):372 (2009)
- Freedom versus constraint in protein function
- Nat Rev Mol Cell Biol 10(6):372 (2009)
- Chromatin remodelling beyond transcription: the INO80 and SWR1 complexes
- Nat Rev Mol Cell Biol 10(6):373-384 (2009)
Chromatin-modifying factors have essential roles in DNA processing pathways that dictate cellular functions. The ability of chromatin modifiers, including the INO80 and SWR1 chromatin-remodelling complexes, to regulate transcriptional processes is well established. However, recent studies reveal that the INO80 and SWR1 complexes have crucial functions in many other essential processes, including DNA repair, checkpoint regulation, DNA replication, telomere maintenance and chromosome segregation. During these diverse nuclear processes, the INO80 and SWR1 complexes function cooperatively with their histone substrates, gamma-H2AX and H2AZ. This research reveals that INO80 and SWR1 ATP-dependent chromatin remodelling is an integral component of pathways that maintain genomic integrity. - The ubiquitin–26S proteasome system at the nexus of plant biology
- Nat Rev Mol Cell Biol 10(6):385-397 (2009)
Plants, like other eukaryotes, rely on proteolysis to control the abundance of key regulatory proteins and enzymes. Strikingly, genome-wide studies have revealed that the ubiquitin-26S proteasome system (UPS) in particular is an exceedingly large and complex route for protein removal, occupying nearly 6% of the Arabidopsis thaliana proteome. But why is the UPS so pervasive in plants? Data accumulated over the past few years now show that it targets numerous intracellular regulators that have central roles in hormone signalling, the regulation of chromatin structure and transcription, tailoring morphogenesis, responses to environmental challenges, self recognition and battling pathogens. - Physiological functions of the HECT family of ubiquitin ligases
- Nat Rev Mol Cell Biol 10(6):398-409 (2009)
The ubiquitylation of proteins is carried out by E1, E2 and E3 (ubiquitin ligase) enzymes, and targets them for degradation or for other cellular fates. The HECT enzymes, including Nedd4 family members, are a major group of E3 enzymes that dictate the specificity of ubiquitylation. In addition to ubiquitylating proteins for degradation by the 26S proteasome, HECT E3 enzymes regulate the trafficking of many receptors, channels, transporters and viral proteins. The physiological functions of the yeast HECT E3 ligase Rsp5 are the best known, but the functions of HECT E3 enyzmes in metazoans are now becoming clearer from in vivo studies. - The second wave of synthetic biology: from modules to systems
Purnick PE Weiss R - Nat Rev Mol Cell Biol 10(6):410-422 (2009)
Synthetic biology is a research field that combines the investigative nature of biology with the constructive nature of engineering. Efforts in synthetic biology have largely focused on the creation and perfection of genetic devices and small modules that are constructed from these devices. But to view cells as true 'programmable' entities, it is now essential to develop effective strategies for assembling devices and modules into intricate, customizable larger scale systems. The ability to create such systems will result in innovative approaches to a wide range of applications, such as bioremediation, sustainable energy production and biomedical therapies. - It takes two to tango: regulation of G proteins by dimerization
- Nat Rev Mol Cell Biol 10(6):423-429 (2009)
Guanine nucleotide-binding (G) proteins, which cycle between a GDP- and a GTP-bound conformation, are conventionally regulated by GTPase-activating proteins (GAPs) and guanine nucleotide-exchange factors (GEFs), and function by interacting with effector proteins in the GTP-bound 'on' state. Here we present another class of G proteins that are regulated by homodimerization, which we would categorize as G proteins activated by nucleotide-dependent dimerization (GADs). This class includes proteins such as signal recognition particle (SRP), dynamin, septins and the newly discovered Roco protein Leu-rich repeat kinase 2 (LRRK2). We propose that the juxtaposition of the G domains of two monomers across the GTP-binding sites activates the biological function of these proteins and the GTPase reaction. - RNA granules: post-transcriptional and epigenetic modulators of gene expression
Anderson P Kedersha N - Nat Rev Mol Cell Biol 10(6):430-436 (2009)
The composition of cytoplasmic messenger ribonucleoproteins (mRNPs) is determined by their nuclear and cytoplasmic histories and reflects past functions and future fates. The protein components of selected mRNP complexes promote their assembly into microscopically visible cytoplasmic RNA granules, including stress granules, processing bodies and germ cell (or polar) granules. We propose that RNA granules can be both a cause and a consequence of altered mRNA translation, decay or editing. In this capacity, RNA granules serve as key modulators of post-transcriptional and epigenetic gene expression.
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