Sonja Vermeren (née Krugmann)
Tel. (01223) 496665

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Research summary

Small GTPases of the Ras superfamily regulate a host of cellular functions including cell motility, adhesion, vesicular transport, cell division and survival. Small GTPases act as molecular switches, cycling between an active, GTP-bound form and an inactive, GDP-bound form. Intrinsic hydrolysis of GTP to GDP is often slow and is catalysed by GTPase activating proteins (GAPs) whilst guanine nucleotide exchange factors (GEFs) catalyse exchange of GDP for GTP.

We recently identified ARAP3 in a screen for novel phosphoinositide 3-OH kinase (PI3K) effectors. ARAP3 is a dual Arf and Rho GAP; it is part of the ARAP family of dual GAPs. ARAP proteins are likely regulator of cross-talk between different families of small G proteins and their regulators such as PI3K. They are likely to have a regulatory role in important cellular functions such as cell motility. Using a mixture of biochemistry and cell biology we characterise the catalytic activities and mode of regulation of ARAP3. Current projects are also underway to elucidate its physiological function in cells.