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Set2 methylation of Lys36 and the recruitment of chromatin remodellers represses histone exchange which limits the incorporation of acetylated histones in coding regions, thereby maintaining chromatin integrity and accurate transcription initiation.
The characterization of dynamic contacts that form between the endoplasmic reticulum and mitochondria have highlighted the different ways in which the functions of these organelles can be coordinated. These structures may also allow co-regulation of distinct processes.
The basic elements of the transforming growth factor-β (TGFβ) pathway came to light more than a decade ago. Since then, the multifunctional nature and medical relevance of this pathway have relentlessly been elucidated. The old mystery of how the context determines the cellular response to TGFβ and its many malfunctions is only starting to be unravelled.
The collective migration of border cells in the Drosophila melanogaster ovary has become a key model for dissecting the mechanisms that govern the coordinated movement of groups of cells. This has implications for our understanding of migration in diverse contexts, including during wound healing and tumour metastasis.
The activity of protein kinases is regulated by domains that are associated with the kinase core, by interacting proteins and by their incorporation into large macromolecular complexes. Thus, understanding kinase signalling requires the structural characterization of entire complexes, as exemplified by studies of cyclic AMP-dependent protein kinase (PKA).
Like nuclear DNA, mitochondrial DNA possesses multiple pathways that function to preserve its integrity following exogenous insults or errors during replication. Because the candidate proteins involved are similar to those carrying out nuclear DNA repair, elucidating the contribution of each repair protein has been challenging.
Research on the cadherin–junctional actin interaction has focused on how the two physically interact. However, the actin cytoskeleton is dynamic, regulated by a network of proteins, so a broader perspective that takes this into account may provide new insights on cadherin cell–cell contacts and on the role of cadherins in disease.
