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.

• PMID: 9188784
• DOI full text
• PubMed
• PubTator

Reference Type

Journal Article

Authors

Ahmadian MR, Mittal R, Hall A, Wittinghofer A

Primary Lit For

Additional Lit For

CDC42

Review For