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Spir proteins nucleate actin polymerization by assembling a linear actin oligomer along a cluster of four actin-binding WH2 domains, and this process is enhanced by formins of the Cappuccino family. The discovery of Spir-like proteins in bacteria indicates that pathogens have adopted this mechanism to manipulate the host actin cytoskeleton.
With a new national science academy, an 'excellence initiative', a roadmap for clinical research and a beefed-up science budget, 2008 looks rosy for German science.
The spatial and temporal regulation of motor-based transport is essential to ensure precise cargo delivery in all cell types. New light has been shed on mechanisms controlling cargo–motor interactions, with the finding that NMDA-cargo is released from KIF17 kinesin following motor phosphorylation by CaMKII near the synapse.
Covalent modifications of histone tails are highly correlated with different states of gene expression. Although the biological significance of many such modifications has been elucidated, the physiological role of Thr 11 phosphorylation on histone H3 (H3T11) has remained elusive.
Successful animal cloning after nuclear transfer requires efficient reprogramming to achieve totipotency. Erasure of pre-existing marks is not always efficient and some genes can escape reprogramming and maintain their original active transcriptional state. Ng and Gurdon propose that the histone H3.3 variant is a key player in this process.
How viruses manage to resist physical and chemical stress and yet open their protective coats during cell infection has been a longstanding, fundamental question. A study with the DNA tumour virus SV40 now shows that protein folding and quality-control factors of the endoplasmic reticulum reshuffle disulfide bonds within the viral capsid, providing a molecular mechanism for the exit of infectious virions from the endoplasmic reticulum.
When cancers spread, they detach from their neighbouring cells and invade the surrounding tissues to reach blood or lymphatic vessels. EGF receptors induce cancer invasion by directly activating GEP100, one of several potential activators of the GTP-binding protein Arf6.
