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an arginine finger, but rather an asparagine (asparagine thumb), which recapitulates Gln61 function ( Daumke et al., 2004 ; Scrima et al., 2008 ). There are several RasGAP with dual Ras and Rap specificity; these include SynGAP [a synaptic protein involved in neuron development ( Kim et al., 2003 )], plexins [transmembrane proteins and receptors for semaphorins that interact with Rap instead of Ras ( Wang et al., 2013 )], and three Gap1 family members [GAP1 IP4BP , Rasal (or Rasal1) and Capri ( Kupzig et al., 2006 ; Sot et al., 2010 )]. The Gap1 family shares a

side chains. It has been speculated that the carboxamide structure is necessary to stabilize the transition state generated by the water attack and has been modeled computationally (Grigorenko et al., 2007). This catalytic carboxamide is often a GTPase residue (e.g., Gln61 in Ras), but in some systems like Rap·RapGAP, the carboxamide is provided by the GAP (Scrima et al., 2008). The Rap GTPase can also be catalyzed by a GAP from the GAP1 family (Kupzig et al., 2006). In the latter case, neither Rap nor GAP1 seems to have a Gln or Asn in the appropriate position

phosphoinositide second messenger lipids (GAP IP4BP , GAP1 m ) with relocation to membranes and an increase in GAP activity (Lockyer et al., 1997, 1999; Cullen and Lockyer, 2002; Sot et al., 2013). However, the exact aspect of Ras signalling regulated by these proteins is unclear. A number of reports have highlighted a potential role of RASAL1 as a tumour suppressor in thyroid, colorectal and hepatocellular tumour progression (Jin et al., 2007; Ohta et al., 2009; Calvisi et al., 2011). Mice deficient for the GAP1 family member CAPRI do not exhibit phenotypic abnormalities if