Ahmadian M R, Mittal R, Hall A, Wittinghofer A
Max-Planck-Institut für molekulare Physiologie, Dortmund, Germany.
FEBS Lett. 1997 May 26;408(3):315-8. doi: 10.1016/s0014-5793(97)00422-5.
AlF4- has long been known to associate with and activate the GDP-bound alpha subunits of heterotrimeric G-proteins. Recently the small guanine nucleotide binding protein Ras has also been shown to associate with AlF4- in the presence of stoichiometric amounts of its GTPase activating protein (GAP). Here we present the isolation of a stable Ras x GDP- x AlF4- x GAP ternary complex by gel filtration. In addition, we generalise the association of AlF4- with the small GTP-binding proteins by demonstrating ternary complex formation for the Cdc42, Rap and Ran proteins in the presence of their respective GAP proteins.
长期以来，人们一直知道AlF4-会与异源三聚体G蛋白的GDP结合型α亚基结合并激活它。最近，在化学计量的GTP酶激活蛋白（GAP）存在的情况下，小GTP结合蛋白Ras也被证明会与AlF4-结合。在此，我们通过凝胶过滤分离出了稳定的Ras·GDP·AlF4-·GAP三元复合物。此外，我们通过证明在各自的GAP蛋白存在的情况下，Cdc42、Rap和Ran蛋白形成三元复合物，从而推广了AlF4-与小GTP结合蛋白的结合情况。
