Volume 8 Issue 4, April 2007

p53 is best known as a tumour suppressor, although recent studies have challenged the view that this is its only role. Instead, p53 has important functions in organismal development, and might contribute to a number of diseases other than cancer.

Histone acetyltransferases (HATs) are highly diverse multiprotein complexes that carry out diverse functions, ranging from repairing regions of DNA damage to maintaining overall genomic integrity. HATs are regulated by associated factors and by the dynamic interplay with existing histone modifications.

Although netrins were identified as migrational cues in the developing central nervous system (CNS), recent work has highlighted previously unrecognized functions of netrins outside the CNS. Netrins regulate diverse processes, such as cell adhesion, motility, proliferation, differentiation and, ultimately, cell survival.

Methylation of histone residues is important for the regulation of gene transcription, epigenetic inheritance and cell fate. Histone methylation was long considered a stable modification, but the recent identification of a histone deiminase and histone demethylases has shown that histone methylation can be dynamically regulated.

Although most proteins contain multiple domains, nearly all folding studies so far have been of single domains in isolation. Here we consider the importance of interdomain cooperativity in protein folding and propose evolutionary mechanisms that prevent misfolding in multidomain proteins.

Recent studies have identified some of the factors that are involved in WNT secretion and have brought the focus of WNT research to the issue of how WNT proteins are secreted. What are the possible mechanisms that underlie this process?