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The tumour suppressor breast and ovarian cancer type 1 susceptibility protein (BRCA1) is integral for the maintenance of genome stability through its roles in cell cycle checkpoint control and DNA repair. Recent studies have revealed the presence of BRCA1 complexes with distinct roles in the DNA damage response.
Formins are highly conserved proteins with essential roles in remodelling the actin and microtubule cytoskeletons. The emerging complexity in the mechanisms governing formin activity mirrors the wide range of essential functions that they perform in cell motility, cell division and cell and tissue morphogenesis.
The pH of individual cellular compartments is independently regulated and highly variable. Molecules that sense the proton concentration and dynamically transport acid and base equivalents stringently regulate pH to ensure that it is maintained at optimal levels for organellar function.
Branched structures are present at all levels of organization in living organisms. Recent studies suggest that cell competition and cell rearrangements might be conserved key features in branch formation that are controlled by local cell signalling events.
How integrins are trafficked by endocytosis markedly affects their distribution and function. Recent studies examining the molecular mechanisms of integrin trafficking show that it affects the recycling of key signalling receptors to influence cellular processes such as cytokinesis, cell migration and tumour angiogenesis.
A single type of dynein motor carries out all minus end-directed microtubule transport in the cytoplasm. Several multifunctional adaptors, including dynactin, LIS1, NUDE and NUDEL, Bicaudal D and RZZ, couple dynein to its wide range of cargos and regulate its function.
G protein-coupled receptors (GPCRs) mediate physiological responses to various hormones, neurotransmitters, sensory stimuli and other ligands. The signalling and trafficking properties of GPCRs are often fine-tuned by receptor-interacting proteins that are differentially expressed in distinct cell types.
Directed evolution optimizes protein function through successive generations of random mutation, artificial selection and screening. This design algorithm provides a reliable approach to engineering proteins with new and useful properties, and helps us to understand how natural evolution occurs.
Most kinesins move processively along microtubules using energy derived from ATP hydrolysis. Almost all of the intermediate structures of this ATPase reaction cycle have been solved for the monomeric kinesin 3 family motor KIF1A. These structures suggest that kinesins might move by a common mechanism.
