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The general election raises the prospect of two or three Finance Acts this year, and some key tax measures are being introduced outside the Finance Bill process. And then there [...]

In April, the PAC began its inquiry into 'the variety of tax reliefs used in the UK and how they are administered' by questioning HMRC chief executive Lin Homer and [...]

Recent high-level developments suggest a growing sense of urgency among officials and lawmakers seeking to reform the international tax system. A broad consensus in favour of change was reflected in [...]

Post‐translational modifications (PTMs) expand the number of protein isoforms in eukaryotic proteome by orders of magnitude. Protein modification with isoprenoid lipids is a common PTM affecting hundreds of proteins controlling the transport of information and materials into, through, and out of the eukaryotic cell. In this modification, a soluble phosphoisoprenoid such as farnesyl (C15) or geranylgeranyl (C20) pyrophosphate moiety is recruited by one of three protein prenyltransferases to covalently modify a C‐terminal cysteine(s) in a target protein. The three mammalian prenyltransferases are farnesyltransferase (FTase), geranylgeranyltransferase type I (GGTase I), and Rab geranylgeranyl transferase (also termed geranylgeranyltransferase type II ‐ GGTase II). In this unit, synthetic isoprenoids conjugated to either a fluorophore or biotin group are used to assay the activity of protein prenyltransferases in vitro or to affinity tag prenylatable proteins in cell lysates. These protocols and their modifications can be used to study the mechanisms of protein prenylation, identify prenylation targets, and characterize inhibitors of protein prenyltransferases in vitro and in vivo. Curr. Protoc. Protein Sci. 62:14.3.1‐14.3.15. © 2010 by John Wiley & Sons, Inc.