Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling Export

@article{citeulike:1512874, abstract = {The ADP-ribosylation factor (Arf) Arf GTPase-activating proteins (GAPs) are a family of proteins that induce hydrolysis of GTP bound to Arf. A conserved domain containing a zinc finger motif mediates catalysis. The substrate, Arf[middle dot]GTP, affects membrane trafficking and actin remodelling. Consistent with activity as an Arf regulator, the Arf GAPs affect both of these pathways. However, the Arf GAPs are likely to have Arf-independent activities that contribute to their cellular functions. Structures of the Arf GAPs are diverse containing catalytic, protein-protein interaction and lipid interaction domains in addition to the Arf GAP domain. Some Arf GAPs have been identified and characterized on the basis of activities other than Arf GAP. Here, we describe the Arf GAP family, enzymology of some members of the Arf GAP family and known functions of the proteins. The results discussed illustrate roles for both Arf-dependent and -independent activities in the regulation of cellular architecture.}, author = {Randazzo, Paul A. and Hirsch, Dianne S.}, citeulike-article-id = {1512874}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cellsig.2003.09.012}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6T2M-4B4HF95-1/2/bb2e0384c4784d7f1ceba90ee30f3820}, doi = {10.1016/j.cellsig.2003.09.012}, journal = {Cellular Signalling}, keywords = {arf, gap}, month = {April}, number = {4}, pages = {401--413}, posted-at = {2007-07-30 14:43:02}, priority = {2}, title = {Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling}, url = {http://dx.doi.org/10.1016/j.cellsig.2003.09.012}, volume = {16}, year = {2004} }

TY - JOUR ID - citeulike:1512874 L3 - citeulike-article-id:1512874 N2 - The ADP-ribosylation factor (Arf) Arf GTPase-activating proteins (GAPs) are a family of proteins that induce hydrolysis of GTP bound to Arf. A conserved domain containing a zinc finger motif mediates catalysis. The substrate, Arf[middle dot]GTP, affects membrane trafficking and actin remodelling. Consistent with activity as an Arf regulator, the Arf GAPs affect both of these pathways. However, the Arf GAPs are likely to have Arf-independent activities that contribute to their cellular functions. Structures of the Arf GAPs are diverse containing catalytic, protein-protein interaction and lipid interaction domains in addition to the Arf GAP domain. Some Arf GAPs have been identified and characterized on the basis of activities other than Arf GAP. Here, we describe the Arf GAP family, enzymology of some members of the Arf GAP family and known functions of the proteins. The results discussed illustrate roles for both Arf-dependent and -independent activities in the regulation of cellular architecture. IS - 4 JF - Cellular Signalling EP - 413 TI - Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling VL - 16 SP - 401 KW - arf KW - gap AU - Randazzo, Paul AU - Hirsch, Dianne PY - 2004/04// UR - http://dx.doi.org/10.1016/j.cellsig.2003.09.012 ER -