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C200481200v1
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Papers In Press, published online ahead of print September 5, 2002
J. Biol. Chem, 10.1074/jbc.C200481200
Submitted on August 23, 2002
Revised on September 5, 2002
Accepted on September 5, 2002

Characterization of a fast-cycling ADP-ribosylation factor 6 mutant

Lorraine C. Santy

Dept. of Cell Biology, Health Sciences Center, University. of Virginia, Charlottesville, VA 22908

Corresponding Author: ls6e{at}virginia.edu

Studies of GTPase function often employ expression of dominant negative or constitutively active mutants. Dominant negative mutants cannot bind GTP and thus cannot be activated. Constitutively active mutants cannot hydrolyze GTP and therefore accumulate a large pool of GTP-bound GTPase. These mutations both block the normal cycle of GTP binding, hydrolysis and release. Therefore although the GTPase deficient mutants are in the active conformation, they do not fully imitate all the actions of the GTPase. This is particularly true for the ADP-ribosylation factors (ARFs), GTPases that regulate vesicular trafficking events. In Ras and Rho GTPases replacement of phenylalanine 28 with a leucine residue produces a “fast-cycling” mutant that can undergo spontaneous GTP-GDP exchange and retains the ability to hydrolyze GTP. Unfortunately this phenylalanine residue is not conserved in the ARF family of GTPases. Here we report the design and characterization of a novel activated mutant of ARF6, ARF6 T157A. In vitro studies show that ARF6 T157A can spontaneously bind and release GTP more quickly than the wild type protein suggesting that it is a fast-cycling mutant. This mutant has enhanced activity in vivo, and induces cortical actin rearrangements in Hela cells and enhanced motility in MDCK cells.


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