Volume 11 Issue 11, November 2010

Intestinal stem cells divide symmetrically and stochastically adopt stem or differentiating fates.

Neural stem and progenitor cell populations are balanced by EGFR-Notch 1.

During pattern formation, cells undergo a dynamic phase of refinement.

Ubiquitin chain trimming by USP14 inhibits protein degradationin vitro and in vivo.

PARP1 acts in a pathway that links feeding to control of peripheral clocks.

Identification of Hos1 as the deacetylase for the cohesin component Smc3.

Anin vitrosystem shows that filopodia can self-assemble.

HMGB1 is a crucial regulator of autophagy.

Transport protein particle (TRAPP; also known as trafficking protein particle) complexes activate the GTPase Ypt1 or RAB1 to regulate membrane traffic in yeast and mammals, respectively. Two different TRAPP complexes tether coated vesicles during endoplasmic reticulum–Golgi and intra-Golgi traffic, respectively, and a third complex functions in autophagy. The TRAPP complexes thereby connect GTPase activation to unique membrane-tethering events.

Organisms can anticipate environmental changes owing to an intrinsic molecular clock. Our molecular understanding of circadian oscillators has advanced over the past decade with the deployment of systems biology approaches, enabling a multiscale view of circadian systems from the molecular level to the intact organism.

The aggregation of misfolded proteins is associated with the perturbation of cellular function and ageing. However, protein aggregation can also be a regulated process that deposits aggregates at specific cellular sites. This is protective as it facilitates aggregate solubilization, refolding and degradation by the protein quality-control network.

Proteomes are typically analyzed by mass spectrometry, and recent advances have greatly increased the fraction of the proteome that can be identified and quantified in a single study. Mapping complete proteomes and using such maps for targeted quantitative proteomics will increase the impact of proteomics on biological and clinical research.

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 how regulatory proteins activate FAK by binding to its FERM domain, enabling it to coordinate diverse cellular responses.