Hot off the presses! Nov 01 Nat Rev Mol Cell Biol

The Nov 01 issue of the Nat Rev Mol Cell Biol is now up on Pubget (About Nat Rev Mol Cell Biol): if you're at a subscribing institution, just click the link in the latest link at the home page. (Note you'll only be able to get all the PDFs in the issue if your institution subscribes to Pubget.)

Latest Articles Include:

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  - Nat Rev Mol Cell Biol 11(11):751 (2010)
  
• Stem cells: Dividing with symmetry | PDF (196 KB)
  - Nat Rev Mol Cell Biol 11(11):752 (2010)
  Intestinal stem cells divide symmetrically and stochastically adopt stem or differentiating fates.
• Stem cells: A balancing act | PDF (225 KB)
  - Nat Rev Mol Cell Biol 11(11):753 (2010)
  Neural stem and progenitor cell populations are balanced by EGFR-Notch 1.
• Checking out the neighbourhood | PDF (174 KB)
  - Nat Rev Mol Cell Biol 11(11):753 (2010)
  During pattern formation, cells undergo a dynamic phase of refinement.
• Protein degradation: Time for trimming | PDF (237 KB)
  - Nat Rev Mol Cell Biol 11(11):754 (2010)
  Ubiquitin chain trimming by USP14 inhibits protein degradation in vitro and in vivo.
• Circadian rhythms: PARP1 feeds into clocks | PDF (408 KB)
  - Nat Rev Mol Cell Biol 11(11):754 (2010)
  PARP1 acts in a pathway that links feeding to control of peripheral clocks.
• Cell cycle: Cycling through acetylation | PDF (296 KB)
  - Nat Rev Mol Cell Biol 11(11):755 (2010)
  Identification of Hos1 as the deacetylase for the cohesin component Smc3.
• Cytoskeleton: Filopodia self-assemble | PDF (289 KB)
  - Nat Rev Mol Cell Biol 11(11):756 (2010)
  An in vitro system shows that filopodia can self-assemble.
• Autophagy: In the hands of HMGB1 | PDF (281 KB)
  - Nat Rev Mol Cell Biol 11(11):756 (2010)
  HMGB1 is a crucial regulator of autophagy.
• Non-coding RNA | Apoptosis | Calcium | PDF (161 KB)
  - Nat Rev Mol Cell Biol 11(11):756 (2010)
  Non-coding RNA Long noncoding RNAs with enhancer-like function in human cells Ørom, U. A. et al. Cell 143, 46â€"58 (2010) Article The biological function of long non-coding RNAs (ncRNAs) is unclear, although those that have been studied in detail silence genes. Ørom et al. observe that, following human primary keratinocyte differentiation, 15% of long ncRNAs show altered expression, and 70% of these are increased.
• In the news | PDF (135 KB)
  - Nat Rev Mol Cell Biol 11(11):757 (2010)
  The Awards season This autumn saw recognition of the crucial contributions that basic research makes to human health, with the announcements of the 2010 Albert Lasker Basic Medical Research Award and Nobel Prize in Physiology or Medicine. Douglas Coleman (The Jackson Laboratory, Bar Harbor, Maine, USA) and Jeffrey Friedman (The Rockefeller University, New York, USA) share the Lasker award for their discovery of the leptin hormone as a key regulator of appetite and body weight.
• TRAPP complexes in membrane traffic: convergence through a common Rab
  - Nat Rev Mol Cell Biol 11(11):759 (2010)
  Transport protein particle (TRAPP; also known as trafficking protein particle), a multimeric guanine nucleotide-exchange factor for the yeast GTPase Ypt1 and its mammalian homologue, RAB1, regulates multiple membrane trafficking pathways. TRAPP complexes exist in three forms, each of which activates Ypt1 or RAB1 through a common core of subunits and regulates complex localization through distinct subunits. Whereas TRAPPI and TRAPPII tether coated vesicles during endoplasmic reticulum to Golgi and intra-Golgi traffic, respectively, TRAPPIII has recently been shown to be reqiured for autophagy. These advances illustrate how the TRAPP complexes link Ypt1 and RAB1 activation to distinct membrane-tethering events.
• Clocks not winding down: unravelling circadian networks
  - Nat Rev Mol Cell Biol 11(11):764 (2010)
  An intrinsic clock enables an organism to anticipate environmental changes and use energy sources more efficiently, thereby conferring an adaptive advantage. Having an intrinsic clock to orchestrate rhythms is also important for human health. The use of systems biology approaches has advanced our understanding of mechanistic features of circadian oscillators over the past decade. The field is now in a position to develop a multiscale view of circadian systems, from the molecular level to the intact organism, and to apply this information for the development of new therapeutic strategies or for enhancing agricultural productivity in crops.
• Cellular strategies for controlling protein aggregation
  - Nat Rev Mol Cell Biol 11(11):777 (2010)
  The aggregation of misfolded proteins is associated with the perturbation of cellular function, ageing and various human disorders. Mounting evidence suggests that protein aggregation is often part of the cellular response to an imbalanced protein homeostasis rather than an unspecific and uncontrolled dead-end pathway. It is a regulated process in cells from bacteria to humans, leading to the deposition of aggregates at specific sites. The sequestration of misfolded proteins in such a way is protective for cell function as it allows for their efficient solubilization and refolding or degradation by components of the protein quality-control network. The organized aggregation of misfolded proteins might also allow their asymmetric distribution to daughter cells during cell division.
• Generating and navigating proteome maps using mass spectrometry
  - Nat Rev Mol Cell Biol 11(11):789 (2010)
  Proteomes, the ensembles of all proteins expressed by cells or tissues, are typically analysed by mass spectrometry. Recent technical and computational advances have greatly increased the fraction of a proteome that can be identified and quantified in a single study. Current mass spectrometry-based proteomic strategies have the potential to reproducibly, accurately, quantitatively and comprehensively measure any protein or whole proteomes from cells and tissues at different states. Achieving these goals will require complete proteome maps and analytical strategies that use these maps as prior information and will greatly enhance the impact of proteomics on biological and clinical research.
• The FERM domain: organizing the structure and function of FAK
  - Nat Rev Mol Cell Biol 11(11):802 (2010)
  Focal adhesion kinase (FAK) is a scaffold and tyrosine kinase protein that binds to itself and cellular partners through its four-point-one, ezrin, radixin, moesin (FERM) domain. Recent structural work reveals that regulatory protein partners convert auto-inhibited FAK into its active state by binding to its FERM domain. Further, the identity of FAK FERM domain-interacting proteins yields clues as to how FAK coordinates diverse cellular responses, including cell adhesion, polarization, migration, survival and death, and suggests that FERM domains might mediate information transfer between the cell cortex and nucleus. Importantly, the FAK FERM domain might act as a paradigm for the actions of other FERM domain-containing proteins.