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Non-random positioning of chromosomal domains in the nucleus is a common feature of eukaryotic genomes and has been linked to transcriptional activity, DNA repair, recombination and stability. Nuclear pores and other integral membrane protein complexes are key players in the dynamic organization of the genome in the nucleus.
Phosphoinositide 3-kinases (PI3Ks), of which there are eight isoforms, function early in intracellular signal transduction pathways and affect many biological functions. Understanding how these isoforms are differentially regulated and how they control signalling might provide new insight into their roles in disease.
The coordinated organization of membrane receptors into diverse micrometre-scale spatial patterns is emerging as an important theme of intercellular signalling, as exemplified by immunological synapses. New experimental strategies have emerged to manipulate the spatial organization of molecules inside living cells.
The link between cytoskeletal actin dynamics and correlated gene activities was unclear. However, the discovery that globular actin polymerization liberates myocardin family transcriptional cofactors to induce serum response factor, which modulates the expression of genes encoding effectors of actin dynamics, has helped bridge this gap in our knowledge.
Leukocytes use different strategies to migrate through the endothelium of venular walls and in interstitial tissues. These strategies are regulated by soluble and cell-bound signals. Studies have identified many of the cellular and subcellular events that govern transendothelial migration and are beginning to elucidate the nature of leukocyte interstitial motility.
GW182 proteins are key components of microRNA silencing complexes in animals, although their precise molecular function has been poorly understood. Recent findings indicate that they promote gene silencing by interfering with cytoplasmic poly(A)-binding protein 1 (PABPC1) function during translation and mRNA stabilization — a mode of action similar to that of PABP-interacting protein 2 (PAIP2).
