Volume 10 Issue 11, November 2009

Alternative splicing is an important gene regulatory mechanism for generating proteomic diversity, which markedly affects human development and is misregulated in many human diseases. Alternative splicing can be regulated at different stages of spliceosome assembly and by different mechanisms.

Ubiquitin-conjugating enzymes (E2s) are major regulators of ubiquitin chain assembly. These enzymes control ubiquitin chain initiation or elongation, the processivity of chain formation and the topology of the assembled chains.

How kinesin motors are regulated in cells to ensure the temporal and spatial fidelity of their microtubule-based activities is poorly understood. Recent work has revealed molecular mechanisms that control kinesin autoinhibition, activation, binding to cargos and microtubule tracks, and localization.

Non-muscle myosin II (NM II) is an actin-binding protein with actin cross-linking and contractile properties. The three mammalian NM II isoforms have both overlapping and distinct roles in cell adhesion and cell migration and their mutation results in specific developmental defects and disease phenotypes.

The evolution of protein–protein interaction and metabolic networks is mostly based on the duplication and loss of entire genes or on point mutations, small insertions or deletions that affect gene regulation. However, network evolution can be understood only when spatiotemporal resolution is taken into account.

During cell division, the asymmetric localization of epigenetic marks and kinetochore proteins might lead to the differential recognition of sister chromatids and the biased segregation of DNA strands to daughter cells. This might ultimately result in the acquisition of distinct cell fates after mitosis.