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Sumoylation is a highly regulated process that is counteracted by specialized enzymes known as small ubiquitin-related modifier (SUMO) proteases. The recent discovery of novel SUMO proteases, together with new findings for established SUMO proteases, has led to augmented appreciation of this enzyme family.
Since the discovery of WNTs 30 years ago, it has become clear that this signalling pathway is incredibly complex, using more than 15 receptors and co-receptors. What has emerged is that these proteins form higher-order ligand–receptor complexes that transduce downstream signalling and influence numerous cellular processes.
In addition to regulating the cascades leading to cell death, mitochondria detect cell stress signals (for example, viral infection) and themselves emit danger signals in response to perturbations of homeostasis to trigger cell-intrinsic or systemic responses. They can therefore be considered as master regulators of danger signalling.
The chromosomal passenger complex (CPC), which is formed by inner centromere protein (INCENP), borealin, survivin and Aurora B kinase, targets to different locations at different times during mitosis. As it regulates key events at each of these locations, the CPC can be considered as a master regulator of mitosis.
Although the physiological importance of adhesion was appreciated early in the twentieth century, understanding its molecular basis was challenging. The development of complementary biochemical and immunological approaches facilitated the discovery of the cadherins, integrins and other major adhesion families and led to the molecular era of adhesion research and the formation of a new research community.